Solution scattering approaches to dynamical ordering in biomolecular systems
Clarification of solution structure and its modulation in proteins and protein complexes is crucially important to understand dynamical ordering in macromolecular systems. Small-angle x-ray scattering (SAXS) and small-angle neutron scattering (SANS) are among the most powerful techniques to derive s...
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| Published in | Biochimica et biophysica acta Vol. 1862; no. 2; pp. 253 - 274 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.02.2018
Elsevier |
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| Online Access | Get full text |
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| Abstract | Clarification of solution structure and its modulation in proteins and protein complexes is crucially important to understand dynamical ordering in macromolecular systems. Small-angle x-ray scattering (SAXS) and small-angle neutron scattering (SANS) are among the most powerful techniques to derive structural information. Recent progress in sample preparation, instruments and software analysis is opening up a new era for small-angle scattering. In this review, recent progress and trends of SAXS and SANS are introduced from the point of view of instrumentation and analysis, touching on general features and standard methods of small-angle scattering. This article is part of a Special Issue entitled “Biophysical Exploration of Dynamical Ordering of Biomolecular Systems” edited by Dr. Koichi Kato.
•Introduction of general theory and classical measuring methods of small-angle X-ray and neutron scattering; SAXS and SANS•Recent progress and trend of small-angle scattering from the viewpoints of instrumentation, analysis method and cutting edge results.•Introduction of SEC-SAXS methods•Recent progress of 3D modeling with SAXS data•Application of contrast variation and deuteration technique for protein systems with SANS |
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| AbstractList | Clarification of solution structure and its modulation in proteins and protein complexes is crucially important to understand dynamical ordering in macromolecular systems. Small-angle x-ray scattering (SAXS) and small-angle neutron scattering (SANS) are among the most powerful techniques to derive structural information. Recent progress in sample preparation, instruments and software analysis is opening up a new era for small-angle scattering. In this review, recent progress and trends of SAXS and SANS are introduced from the point of view of instrumentation and analysis, touching on general features and standard methods of small-angle scattering. This article is part of a Special Issue entitled “Biophysical Exploration of Dynamical Ordering of Biomolecular Systems” edited by Dr. Koichi Kato. Clarification of solution structure and its modulation in proteins and protein complexes is crucially important to understand dynamical ordering in macromolecular systems. Small-angle x-ray scattering (SAXS) and small-angle neutron scattering (SANS) are among the most powerful techniques to derive structural information. Recent progress in sample preparation, instruments and software analysis is opening up a new era for small-angle scattering. In this review, recent progress and trends of SAXS and SANS are introduced from the point of view of instrumentation and analysis, touching on general features and standard methods of small-angle scattering. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.Clarification of solution structure and its modulation in proteins and protein complexes is crucially important to understand dynamical ordering in macromolecular systems. Small-angle x-ray scattering (SAXS) and small-angle neutron scattering (SANS) are among the most powerful techniques to derive structural information. Recent progress in sample preparation, instruments and software analysis is opening up a new era for small-angle scattering. In this review, recent progress and trends of SAXS and SANS are introduced from the point of view of instrumentation and analysis, touching on general features and standard methods of small-angle scattering. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato. Clarification of solution structure and its modulation in proteins and protein complexes is crucially important to understand dynamical ordering in macromolecular systems. Small-angle x-ray scattering (SAXS) and small-angle neutron scattering (SANS) are among the most powerful techniques to derive structural information. Recent progress in sample preparation, instruments and software analysis is opening up a new era for small-angle scattering. In this review, recent progress and trends of SAXS and SANS are introduced from the point of view of instrumentation and analysis, touching on general features and standard methods of small-angle scattering. This article is part of a Special Issue entitled “Biophysical Exploration of Dynamical Ordering of Biomolecular Systems” edited by Dr. Koichi Kato. •Introduction of general theory and classical measuring methods of small-angle X-ray and neutron scattering; SAXS and SANS•Recent progress and trend of small-angle scattering from the viewpoints of instrumentation, analysis method and cutting edge results.•Introduction of SEC-SAXS methods•Recent progress of 3D modeling with SAXS data•Application of contrast variation and deuteration technique for protein systems with SANS |
| Author | Zaccai, Giuseppe Kamikubo, Hironari Shimizu, Nobutaka Bernadó, Pau Sugiyama, Masaaki |
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| Cites_doi | 10.1093/nar/gkr430 10.1016/j.bpj.2011.10.046 10.1107/S0021889812007662 10.1186/1471-2105-11-429 10.1021/ja808490b 10.1093/nar/gkv1466 10.1016/j.bpj.2012.01.002 10.1016/j.chroma.2009.02.053 10.1007/s00249-009-0549-3 10.1016/j.str.2016.10.013 10.1002/pro.83 10.1038/srep38399 10.1107/S0021889895007047 10.1016/j.jmb.2016.02.007 10.1038/srep35567 10.1524/zpch.1970.72.4_6.177 10.1021/jacs.5b07765 10.1002/prot.23033 10.1038/srep30287 10.1016/S0006-3495(99)77443-6 10.1002/pro.587 10.1107/S0021889886089513 10.1016/j.sbi.2013.06.007 10.1016/j.str.2010.10.006 10.1021/ja1063923 10.1002/pro.435 10.1002/bip.1981.360201110 10.1016/j.bpj.2011.09.004 10.1093/nar/gkq461 10.1126/science.aag2516 10.1107/S1600576716011201 10.1021/acs.chemrev.5b00548 10.1111/j.1432-1033.1983.tb07475.x 10.1529/biophysj.107.113167 10.1016/0022-2836(81)90417-4 10.1093/nar/gkw389 10.1016/j.sbi.2016.05.003 10.1107/S1600576716016514 10.1039/C1MB05275F 10.1002/0471140864.ps1714s70 10.1093/nar/gkv368 10.1073/pnas.012458999 10.5936/csbj.201308006 10.1529/biophysj.107.122218 10.1016/j.bpj.2013.07.020 10.1529/biophysj.105.064154 10.1107/S1399004714018446 10.1107/S1600577516015083 10.1093/nar/gkv309 10.1016/j.bpj.2014.04.007 10.1016/bs.mie.2015.06.014 10.1107/S0021889874009071 10.1107/S010876731104788X 10.1016/j.bpj.2014.06.006 10.1111/febs.12772 10.1021/ja069124n 10.1021/acs.jpclett.5b02399 10.1016/j.molcel.2008.01.015 10.1073/pnas.0808903105 10.1107/S0021889809000338 10.1088/0034-4885/39/10/001 10.1038/srep40948 10.1016/j.sbi.2012.07.014 10.1073/pnas.69.8.1997 10.1093/nar/gkw1183 10.1107/S0021889811035758 10.1093/nar/2.11.2163 10.1093/nar/4.11.3769 10.1007/BF01394523 10.1021/ja106173n 10.1107/S0021889803000268 10.1107/S1600576715010420 10.1007/978-3-319-20164-1_8 10.1107/S0909049504019272 10.1016/S0006-3495(98)77984-6 10.1016/j.bpj.2015.03.062 10.1016/j.bpj.2010.08.017 10.1103/PhysRevLett.98.238101 10.1107/S0021889896013398 10.1107/S0021889809029288 10.1039/C5CP04886A 10.1038/srep29208 10.1016/S0003-2670(03)00724-4 10.1021/pr060594q 10.1016/0022-2836(78)90042-6 10.1107/S0108767396000177 10.1039/C1MB05243H 10.1073/pnas.1004569107 10.1107/S0021889803012779 10.4149/gpb_2009_02_174 10.1016/j.jsb.2010.09.023 10.1107/S0021889897002173 10.1021/ja301667n 10.1107/S205225251500202X 10.1016/j.sbi.2016.10.011 10.1006/jmbi.2001.4611 10.1016/j.jmb.2010.08.029 10.1016/0022-2836(84)90338-3 10.1107/S1600576713033475 10.1107/S2052252516016018 10.1016/0921-4526(92)90524-V 10.1038/nprot.2016.113 10.1006/jmbi.1996.0491 10.1063/1.4952937 10.1017/S0033583507004635 10.2174/138920312799277901 10.1021/bi00420a051 10.1021/bi980535t 10.1107/S1399004715002576 10.1016/j.bpj.2012.12.019 10.1016/S0006-3495(86)83573-1 10.1107/S0909049504014086 10.1039/C5CP04540A |
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| Keywords | SEC-SANS Hybrid method Deuteration Ab-initio modeling CV-SANS |
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| References | Putnam, Lowe, Meiler (bb0190) 2013; 8 Csizmok, Follis, Kriwacki, Forman-Kay (bb0285) 2016; 116 Antonov, Olsson, Boomsma, Hamelryck (bb0340) 2016; 18 Shimizu, Yatabe, Nagatani, Saijyo, Kosuge, Igarashi (bb0085) 2016; 1741 Konarev, Volkov, Sokolova, Koch, Svergun (bb0620) 2003; 36 I. N. Serdyuk, N. R. Zaccai, J. Zaccai, Methods in Molecular Biophysics: Structure, Dynamics, Function, Cambridge University Press. Chen, Hodgson, Doniach (bb0385) 1996; 261 David, Pérez (bb0040) 2009; 42 Schneidman-Duhovny, Hammel, Sali (bb0215) 2011; 173 bb0430 Jacrot (bb0490) 1976; 39 Stovgaard, Andreetta, Ferkinghoff-Borg, Hamelryck (bb0155) 2010; 11 Kjaergaard, Nørholm, Hendus-Altenburger, Pedersen, Poulsen, Kragelund (bb0350) 2010; 19 Smolin, Biehl, Kneller, Richter, Smith (bb0450) 2012; 102 Graewert, Svergun (bb0005) 2013; 23 Rozycki, Kim, Hummer (bb0330) 2011; 19 Daughdrill, Kashtanov, Stancik, Hill, Helms, Muschol, Receveur-Bréchot, Ytreberg (bb0335) 2012; 8 Inoue, Biehl, Rosenkranz, Fitter, Monkenbusch, Radulescu, Farago, Richter (bb0445) 2010; 99 Pelikan, Hura, Hammel (bb0315) 2009; 28 Trygg, Holmes, Lundstedt (bb0370) 2007; 6 . Jeffries, Graewert, Blanchet, Langley, Whitten, Svergun (bb0080) 2016; 11 Blobel, Bernadó, Svergun, Tauler, Pons (bb0380) 2009; 131 Svergun, Volkov, Kozin, Stuhrmann (bb0115) 1996; 52 Stuhrmann (bb0110) 1970; 70 Sugiyama, Horikoshi, Suzuki, Taguchi, Kujirai, Inoue, Oba, Sato, Martel, Porcar, Kurumizaka (bb0535) 2015; 4 Engelman, Moore (bb0545) 1972; 69 Sugiyama, Arimura, Shirayama, Fujita, Oba, Sato, Inoue, Oda, Sato, Heenan, Kurumizaka (bb0530) 2014; 106 Inoue, Takata, Fujii, Ishii, Uchiyama, Sato, Oba, Wood, Kato, Fujii, Sugiyama (bb0605) 2016; 6 Leclerc, Zaccai, Vergne, Rihova, Martel, Maurel (bb0505) 2016; 6 Moore, Capel, Kjeldgaard, Engelman (bb0560) 1986; 49 Svergun, Barberato, Koch (bb0150) 1995; 28 Bernadó (bb0240) 2010; 39 Tseng, Goularte, Chavan, Luu, Cohen, Chang, Heisler, Li, Michael, Tripathi, Golden, LiWang, Partch (bb0590) 2017; 355 Mathew, Mirza, Menhart (bb0035) 2004; 11 Botte, Zaccai, Nijeholt, Martin, Knoops, Papai, Zou, Deniaud, Karuppasamy, Jiang, Roy, Schulten, Schultz, Rappsilber, Zaccai, Berger, Collinson, Schaffitzel (bb0485) 2016; 6 Petoukhov, Franke, Shkumatov, Tria, Kikhney, Gajda, Gorba, Mertens, Konarev, Svergun (bb0265) 2012; 45 Schneidman-Duhovny, Hammel, Tainer, Sali (bb0180) 2013; 105 Chen, Hub (bb0195) 2014; 107 Heenan, Penfold, King (bb0465) 1997; 30 Putnam, Hammel, Hura, Tainer (bb0010) 2007; 40 Akiyama, Nohara, Ito, Maéda (bb0415) 2008; 29 Receveur-Brechot, Durand (bb0295) 2012; 13 Jiménez-García, Pons, Svergun, Bernadó, Fernández-Recio (bb0230) 2015; 43 SCÅTTER – software for the analysis of biological SAXS datasets Al-Zyoud, Hynson, Ganuelas, Coster, Duff, Baker, Stewart, Giannoulatou, Ho, Gaus, Liu, Lee (bb0060) 2016; 44 Brooks-Bartlett, Batters, Bury, Lowe, Ginn, Roundc, Garman (bb0030) 2017; 24 Schneidman-Duhovny, Hammel, Sali (bb0185) 2010; 38 Bernadó, Mylonas, Petoukhov, Blackledge, Svergun (bb0305) 2007; 129 Evrard, Mareuil, Bontems, Sizun, Perez (bb0235) 2011; 44 de Juan, Tauler (bb0365) 2003; 500 Chen, Hub (bb0275) 2015; 6 Akiyama, Takahashi, Kimura, Ishimori, Morishima, Nishikawa, Fujisawa (bb0400) 2002; 99 Feigin, Svergun (bb0480) 1987 Malaby, Chakravarthy, Irving, Kathuria, Bilselb, Lambright (bb0100) 2015; 48 Zhao, Speir, Matsui, Lin, Liang, Lynn, Varnado, Weiss, Tang (bb0065) 2016; 11 Pardon, Worcester, Richards (bb0510) 1975; 2 Appolaire, Girard, Colombo, Asunción Durá, Moulin, Härtlein, Franzettia, Gabel (bb0570) 2014; 70 Jacrot, Zaccai (bb0495) 1981; 20 Pérez, Nishino (bb0055) 2012; 22 Gunn, Gorman, Dobson, Parker, Mulhern (bb0050) 2011; F67 Kuwamoto, Akiyama, Fujisawa (bb0020) 2004; 11 Williamson, Craig, Kondrashkina, Bailey-Kellogg, Friedman (bb0375) 2008; 94 Tuukkanen, Svergun (bb0260) 2014; 281 Petoukhov, Svergun (bb0210) 2005; 89 Dessen, Blanquet, Zaccai, Jacrot (bb0500) 1978; 126 Yu Srrmmst, Moore (bb0550) 1981; 153 bb0475 You can get a visual image from Mezei (bb0440) 1972; 255 Nakano, Fukuda, Kudo, Endo, Handa (bb0610) 2007; 98 P. Lindner, R. P. May, P. A. Timmins, Upgrading of the SANS instrument D11 at the ILL, Physica B, 180–181 (1992) 967–972. Hirai, Niimura, Zama, Mita, Ichimura, Tokunaga, Ishikawa (bb0525) 1998; 27 Bertini, Giachetti, Luchinat, Parigi, Petoukhov, Pierattelli, Ravera, Svergun (bb0325) 2010; 132 Bernadó, Pérez, Blobel, Fernández-Recio, Svergun, Pons (bb0270) 2009; 18 Sugiyama, Yagi, Ishii, Porcar, Martel, Oyama, Noda, Yunoki, Murakami, Inoue, Sato, Oba, Terauchi, Uchiyama, Kato (bb0580) 2016; 6 Grishaev (bb0025) 2012; 70 (bb0435) 2005 Sibbet, Carpenter, Baldwin (bb0520) 1983; 133 Bernadó, Svergun (bb0290) 2012; 8 Leyrat, Jensen, Ribeiro, Gérard, Ruigrok, Blackledge, Jamin (bb0355) 2011; 20 Franke, Svergun (bb0130) 2009; 42 Tuukkanen, Kleywegt, Svergun (bb0145) 2016; 3 Cordeiro, Chen, De Biasio, Sibille, Blanco, Hub, Crehuet, Bernadó (bb0205) 2017; 47 Kachala, Valentini, Svergun (bb0300) 2015; 870 Herranz-Trillo, Groenning, van Maarschalkerweerd, Tauler, Vestergaard, Bernadó (bb0405) 2017; 25 Suau, Kneale, Bradbury (bb0515) 1977; 4 Whitten, Jeffries, Harrisc, Trewhella (bb0595) 2008; 105 Yogo, Yanaka, Yagi, Martel, Porcar, Ueki, Inoue, Sato, Sugiyama, Kato (bb0585) 2017; 12 Pérez, Vachette, Russo, Desmadril, Durand (bb0395) 2001; 308 Ishikawa, Furusaka, Nimura, Arai, Hasegawa (bb0460) 1986; 19 Petoukhov, Franke, Shkumatov, Tria, Kikhney, Gajda, Gorba, Mertens, Konarev, Svergun (bb0090) 2012; 45 Volkov, Svergun (bb0135) 2003; 36 Berthaud, Manzi, Pérez, Mangenot (bb0070) 2012; 134 Grishaev, Guo, Irving, Bax (bb0160) 2010; 132 Liu, Morris, Hexemer, Grandison, Zwart (bb0170) 2012; 68 Segel, Fink, Hodgson, Doniach (bb0390) 1998; 37 Chacón, Morán, Díaz, Pantos, Andreu (bb0120) 1998; 74 Shkumatov, Chinnathambi, Mandelkow, Svergun (bb0345) 2011; 79 Ibrahim, Martel, Moulin, Kim, Härtlein, Franzetti, Gabel (bb0615) 2017; 7 Pons, D'Abramo, Svergun, Orozco, Bernadó, Fernández-Recio (bb0225) 2010; 403 Yang, Blachowicz, Makowski, Roux (bb0320) 2010; 107 Gorba, Miyashita, Tama (bb0245) 2008; 94 Poitevin, Orland, Doniach, Koehl, Delarue (bb0175) 2011; 39 Toma-Fukai, Kim, Park, Kuwabara, Shimizu, Krayukhina, Uchiyama, Fukamizu, Shimizu (bb0075) 2016; 428 Duff, Wilde, Rekas, Lake, Holden (bb0565) 2015; 565 Jordan, Jacques, Merrick, Devos, Trevor Forsyth, Porcar, Martel (bb0625) 2016; 49 Sugiyama, Yagi, Yamaguchi, Kumoi, Hirai, Oba, Sato, Porcar, Martel, Kato (bb0575) 2014; 47 Knight, Hub (bb0200) 2015; 43 Panjkovich, Svergun (bb0250) 2016; 18 Cordeiro, Herranz-Trillo, Urbanek, Estaña, Cortés, Sibille, Bernadó (bb0360) 2017; 42 Watanabe, Inoko (bb0045) 2009; 1216 Minh, Makowski (bb0410) 2013; 104 Brookes, Vachette, Rocco, Pérez (bb0095) 2016; 49 Sugiyama, Kurimoto, Yagi, Mori, Fukunaga, Hirai, Zaccai, Kato (bb0600) 2011; 110 Chen, Hub (bb0255) 2015; 108 Svergun (bb0125) 1999; 76 Petoukhov, Svergun (bb0140) 2015; 71 Ramakrishnan, Capel, Kjeldgaard, Engelman, Moore (bb0555) 1984; 174 Trewhella (bb0015) 2016; 40 Schneidman-Duhovny, Hammel, Tainer, Sali (bb0220) 2016; 44 Thiyagarajan, Epperson, Crawford, Carpenter, Klippert, Wozniak (bb0470) 1997; 30 Stuhrmann (bb0540) 1974; 7 Delaforge, Milles, Bouvignies, Bouvier, Boivin, Salvi, Maurin, Martel, Round, Lemke, Jensen, Hart, Blackledge (bb0280) 2015; 137 dos Reis, Aparicio, Zhang (bb0165) 2011; 101 Tria, Mertens, Kachala, Svergun (bb0310) 2015; 2 Bertini (10.1016/j.bbagen.2017.10.015_bb0325) 2010; 132 Malaby (10.1016/j.bbagen.2017.10.015_bb0100) 2015; 48 Rozycki (10.1016/j.bbagen.2017.10.015_bb0330) 2011; 19 Pons (10.1016/j.bbagen.2017.10.015_bb0225) 2010; 403 Svergun (10.1016/j.bbagen.2017.10.015_bb0115) 1996; 52 Al-Zyoud (10.1016/j.bbagen.2017.10.015_bb0060) 2016; 44 Petoukhov (10.1016/j.bbagen.2017.10.015_bb0090) 2012; 45 Leyrat (10.1016/j.bbagen.2017.10.015_bb0355) 2011; 20 Segel (10.1016/j.bbagen.2017.10.015_bb0390) 1998; 37 Blobel (10.1016/j.bbagen.2017.10.015_bb0380) 2009; 131 10.1016/j.bbagen.2017.10.015_bb0425 Feigin (10.1016/j.bbagen.2017.10.015_bb0480) 1987 Mezei (10.1016/j.bbagen.2017.10.015_bb0440) 1972; 255 Jeffries (10.1016/j.bbagen.2017.10.015_bb0080) 2016; 11 10.1016/j.bbagen.2017.10.015_bb0420 Franke (10.1016/j.bbagen.2017.10.015_bb0130) 2009; 42 Jordan (10.1016/j.bbagen.2017.10.015_bb0625) 2016; 49 Stovgaard (10.1016/j.bbagen.2017.10.015_bb0155) 2010; 11 Liu (10.1016/j.bbagen.2017.10.015_bb0170) 2012; 68 Sibbet (10.1016/j.bbagen.2017.10.015_bb0520) 1983; 133 Inoue (10.1016/j.bbagen.2017.10.015_bb0605) 2016; 6 Chacón (10.1016/j.bbagen.2017.10.015_bb0120) 1998; 74 Herranz-Trillo (10.1016/j.bbagen.2017.10.015_bb0405) 2017; 25 Dessen (10.1016/j.bbagen.2017.10.015_bb0500) 1978; 126 Graewert (10.1016/j.bbagen.2017.10.015_bb0005) 2013; 23 Whitten (10.1016/j.bbagen.2017.10.015_bb0595) 2008; 105 Panjkovich (10.1016/j.bbagen.2017.10.015_bb0250) 2016; 18 Akiyama (10.1016/j.bbagen.2017.10.015_bb0400) 2002; 99 Leclerc (10.1016/j.bbagen.2017.10.015_bb0505) 2016; 6 Daughdrill (10.1016/j.bbagen.2017.10.015_bb0335) 2012; 8 Suau (10.1016/j.bbagen.2017.10.015_bb0515) 1977; 4 Knight (10.1016/j.bbagen.2017.10.015_bb0200) 2015; 43 Stuhrmann (10.1016/j.bbagen.2017.10.015_bb0110) 1970; 70 Svergun (10.1016/j.bbagen.2017.10.015_bb0125) 1999; 76 Kuwamoto (10.1016/j.bbagen.2017.10.015_bb0020) 2004; 11 Thiyagarajan (10.1016/j.bbagen.2017.10.015_bb0470) 1997; 30 Smolin (10.1016/j.bbagen.2017.10.015_bb0450) 2012; 102 Tuukkanen (10.1016/j.bbagen.2017.10.015_bb0260) 2014; 281 Shkumatov (10.1016/j.bbagen.2017.10.015_bb0345) 2011; 79 Sugiyama (10.1016/j.bbagen.2017.10.015_bb0580) 2016; 6 Brooks-Bartlett (10.1016/j.bbagen.2017.10.015_bb0030) 2017; 24 Kjaergaard (10.1016/j.bbagen.2017.10.015_bb0350) 2010; 19 Ramakrishnan (10.1016/j.bbagen.2017.10.015_bb0555) 1984; 174 Brookes (10.1016/j.bbagen.2017.10.015_bb0095) 2016; 49 dos Reis (10.1016/j.bbagen.2017.10.015_bb0165) 2011; 101 Trygg (10.1016/j.bbagen.2017.10.015_bb0370) 2007; 6 Berthaud (10.1016/j.bbagen.2017.10.015_bb0070) 2012; 134 Yu Srrmmst (10.1016/j.bbagen.2017.10.015_bb0550) 1981; 153 Nakano (10.1016/j.bbagen.2017.10.015_bb0610) 2007; 98 Jacrot (10.1016/j.bbagen.2017.10.015_bb0490) 1976; 39 Delaforge (10.1016/j.bbagen.2017.10.015_bb0280) 2015; 137 Pérez (10.1016/j.bbagen.2017.10.015_bb0395) 2001; 308 Bernadó (10.1016/j.bbagen.2017.10.015_bb0270) 2009; 18 10.1016/j.bbagen.2017.10.015_bb0455 Bernadó (10.1016/j.bbagen.2017.10.015_bb0290) 2012; 8 Zhao (10.1016/j.bbagen.2017.10.015_bb0065) 2016; 11 Duff (10.1016/j.bbagen.2017.10.015_bb0565) 2015; 565 Gunn (10.1016/j.bbagen.2017.10.015_bb0050) 2011; F67 Grishaev (10.1016/j.bbagen.2017.10.015_bb0160) 2010; 132 Csizmok (10.1016/j.bbagen.2017.10.015_bb0285) 2016; 116 Kachala (10.1016/j.bbagen.2017.10.015_bb0300) 2015; 870 Stuhrmann (10.1016/j.bbagen.2017.10.015_bb0540) 1974; 7 Tuukkanen (10.1016/j.bbagen.2017.10.015_bb0145) 2016; 3 Cordeiro (10.1016/j.bbagen.2017.10.015_bb0360) 2017; 42 Petoukhov (10.1016/j.bbagen.2017.10.015_bb0210) 2005; 89 Sugiyama (10.1016/j.bbagen.2017.10.015_bb0530) 2014; 106 Pérez (10.1016/j.bbagen.2017.10.015_bb0055) 2012; 22 Trewhella (10.1016/j.bbagen.2017.10.015_bb0015) 2016; 40 10.1016/j.bbagen.2017.10.015_bb0105 Jiménez-García (10.1016/j.bbagen.2017.10.015_bb0230) 2015; 43 Toma-Fukai (10.1016/j.bbagen.2017.10.015_bb0075) 2016; 428 Antonov (10.1016/j.bbagen.2017.10.015_bb0340) 2016; 18 Schneidman-Duhovny (10.1016/j.bbagen.2017.10.015_bb0215) 2011; 173 Receveur-Brechot (10.1016/j.bbagen.2017.10.015_bb0295) 2012; 13 Chen (10.1016/j.bbagen.2017.10.015_bb0385) 1996; 261 Petoukhov (10.1016/j.bbagen.2017.10.015_bb0140) 2015; 71 Schneidman-Duhovny (10.1016/j.bbagen.2017.10.015_bb0220) 2016; 44 Svergun (10.1016/j.bbagen.2017.10.015_bb0150) 1995; 28 Konarev (10.1016/j.bbagen.2017.10.015_bb0620) 2003; 36 Schneidman-Duhovny (10.1016/j.bbagen.2017.10.015_bb0180) 2013; 105 Ibrahim (10.1016/j.bbagen.2017.10.015_bb0615) 2017; 7 Ishikawa (10.1016/j.bbagen.2017.10.015_bb0460) 1986; 19 Gorba (10.1016/j.bbagen.2017.10.015_bb0245) 2008; 94 Chen (10.1016/j.bbagen.2017.10.015_bb0255) 2015; 108 (10.1016/j.bbagen.2017.10.015_bb0435) 2005 Engelman (10.1016/j.bbagen.2017.10.015_bb0545) 1972; 69 de Juan (10.1016/j.bbagen.2017.10.015_bb0365) 2003; 500 Tria (10.1016/j.bbagen.2017.10.015_bb0310) 2015; 2 Cordeiro (10.1016/j.bbagen.2017.10.015_bb0205) 2017; 47 Sugiyama (10.1016/j.bbagen.2017.10.015_bb0535) 2015; 4 Tseng (10.1016/j.bbagen.2017.10.015_bb0590) 2017; 355 Grishaev (10.1016/j.bbagen.2017.10.015_bb0025) 2012; 70 Schneidman-Duhovny (10.1016/j.bbagen.2017.10.015_bb0185) 2010; 38 Yang (10.1016/j.bbagen.2017.10.015_bb0320) 2010; 107 Petoukhov (10.1016/j.bbagen.2017.10.015_bb0265) 2012; 45 Inoue (10.1016/j.bbagen.2017.10.015_bb0445) 2010; 99 Mathew (10.1016/j.bbagen.2017.10.015_bb0035) 2004; 11 Sugiyama (10.1016/j.bbagen.2017.10.015_bb0575) 2014; 47 Bernadó (10.1016/j.bbagen.2017.10.015_bb0240) 2010; 39 Putnam (10.1016/j.bbagen.2017.10.015_bb0190) 2013; 8 Botte (10.1016/j.bbagen.2017.10.015_bb0485) 2016; 6 Sugiyama (10.1016/j.bbagen.2017.10.015_bb0600) 2011; 110 Hirai (10.1016/j.bbagen.2017.10.015_bb0525) 1998; 27 Evrard (10.1016/j.bbagen.2017.10.015_bb0235) 2011; 44 Jacrot (10.1016/j.bbagen.2017.10.015_bb0495) 1981; 20 David (10.1016/j.bbagen.2017.10.015_bb0040) 2009; 42 Bernadó (10.1016/j.bbagen.2017.10.015_bb0305) 2007; 129 Minh (10.1016/j.bbagen.2017.10.015_bb0410) 2013; 104 Akiyama (10.1016/j.bbagen.2017.10.015_bb0415) 2008; 29 Pardon (10.1016/j.bbagen.2017.10.015_bb0510) 1975; 2 Appolaire (10.1016/j.bbagen.2017.10.015_bb0570) 2014; 70 Chen (10.1016/j.bbagen.2017.10.015_bb0195) 2014; 107 Shimizu (10.1016/j.bbagen.2017.10.015_bb0085) 2016; 1741 Putnam (10.1016/j.bbagen.2017.10.015_bb0010) 2007; 40 Heenan (10.1016/j.bbagen.2017.10.015_bb0465) 1997; 30 Yogo (10.1016/j.bbagen.2017.10.015_bb0585) 2017; 12 Moore (10.1016/j.bbagen.2017.10.015_bb0560) 1986; 49 Pelikan (10.1016/j.bbagen.2017.10.015_bb0315) 2009; 28 Volkov (10.1016/j.bbagen.2017.10.015_bb0135) 2003; 36 Chen (10.1016/j.bbagen.2017.10.015_bb0275) 2015; 6 Williamson (10.1016/j.bbagen.2017.10.015_bb0375) 2008; 94 Watanabe (10.1016/j.bbagen.2017.10.015_bb0045) 2009; 1216 Poitevin (10.1016/j.bbagen.2017.10.015_bb0175) 2011; 39 |
| References_xml | – volume: 428 start-page: 1197 year: 2016 end-page: 1208 ident: bb0075 article-title: Novel helical assembly in arginine methyltransferase 8 publication-title: J. Mol. Biol. – volume: 403 start-page: 217 year: 2010 end-page: 230 ident: bb0225 article-title: Structural characterization of protein-protein complexes by integrating computational docking with small-angle scattering data publication-title: J. Mol. Biol. – volume: 29 start-page: 703 year: 2008 end-page: 716 ident: bb0415 article-title: Assembly and disassembly dynamics of the cyanobacterial periodosome publication-title: Mol. Cell – volume: 18 start-page: 716 year: 2009 end-page: 726 ident: bb0270 article-title: Structural characterization of unphosphorylated STAT5a oligomerization equilibrium in solution by small-angle X-ray scattering publication-title: Protein Sci. – volume: 8 start-page: 1 year: 2013 end-page: 12 ident: bb0190 article-title: Reconstruction of Saxs profiles from protein structures publication-title: Comput. Struct. Biotechnol. J. – volume: 71 start-page: 1051 year: 2015 end-page: 1058 ident: bb0140 article-title: Ambiguity assessment of small-angle scattering curves from monodisperse systems publication-title: Acta Crystallogr. Sect. D: Biol. Crystallogr. – volume: 1741 year: 2016 ident: bb0085 article-title: Software development for analysis of small-angle X-ray scattering data publication-title: AIP Conf. Proc. – volume: 7 start-page: 40948 year: 2017 ident: bb0615 article-title: Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA publication-title: Sci Rep – volume: 126 start-page: 293 year: 1978 end-page: 313 ident: bb0500 article-title: Antico-operative binding of initiator transfer RNAMet to methionyl-transfer RNA synthetase from publication-title: J. Mol. Biol. – volume: 8 start-page: 308 year: 2012 end-page: 319 ident: bb0335 article-title: Understanding the structural ensembles of a highly extended disordered protein publication-title: Mol. BioSyst. – volume: 6 start-page: 469 year: 2007 end-page: 479 ident: bb0370 article-title: Chemometrics in metabonomics publication-title: J. Proteome Res. – volume: 132 start-page: 15484 year: 2010 end-page: 15486 ident: bb0160 article-title: Improved fitting of solution X-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling publication-title: J. Am. Chem. Soc. – volume: 105 start-page: 962 year: 2013 end-page: 974 ident: bb0180 article-title: Accurate SAXS profile computation and its assessment by contrast variation experiments publication-title: Biophys. J. – volume: 47 start-page: 1501 year: 2017 end-page: 1515 ident: bb0205 article-title: Disentangling polydispersity in the PCNA-p15PAF complex, a disordered, transient and multivalent macromolecular assembly publication-title: Nucleic Acids Res. – volume: 131 start-page: 4378 year: 2009 end-page: 4386 ident: bb0380 article-title: Low-resolution structures of transient protein-protein complexes using small-angle X-ray scattering publication-title: J. Am. Chem. Soc. – volume: 6 start-page: 35567 year: 2016 ident: bb0580 article-title: Structural characterization of the circadian clock protein complex composed of KaiB and KaiC by inverse contrast-matching small-angle neutron scattering publication-title: Sci Rep – volume: 40 start-page: 191 year: 2007 end-page: 285 ident: bb0010 article-title: X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution publication-title: Q. Rev. Biophys. – volume: 18 start-page: 5707 year: 2016 end-page: 5719 ident: bb0250 article-title: Deciphering conformational transitions of proteins by small angle X-ray scattering and normal mode analysis publication-title: Phys. Chem. Chem. Phys. – volume: 6 start-page: 5116 year: 2015 end-page: 5121 ident: bb0275 article-title: Structural properties of protein-detergent complexes from SAXS and MD simulations publication-title: J. Phys. Chem. Lett. – volume: 38 start-page: W540 year: 2010 end-page: W544 ident: bb0185 article-title: FoXS: a web server for rapid computation and fitting of SAXS profiles publication-title: Nucleic Acids Res. – volume: 45 start-page: 342 year: 2012 end-page: 350 ident: bb0265 article-title: New developments in the ATSAS program package for small-angle scattering data analysis publication-title: J. Appl. Crystallogr. – year: 2005 ident: bb0435 article-title: Neutron Scattering from Magnetic Materials 1st Edition publication-title: Elsevier – volume: 13 start-page: 55 year: 2012 end-page: 75 ident: bb0295 article-title: How random are intrinsically disordered proteins? A small angle scattering perspective publication-title: Curr. Protein Pept. Sci. – volume: 2 start-page: 2163 year: 1975 end-page: 2176 ident: bb0510 article-title: Low-angle neutron scattering from chromatin subunit particles publication-title: Nucleic Acids Res. – reference: SCÅTTER – software for the analysis of biological SAXS datasets: – volume: 48 start-page: 1102 year: 2015 end-page: 1113 ident: bb0100 article-title: Methods for analysis of size-exclusion chromatography–small-angle X-ray scattering and reconstruction of protein scattering publication-title: J. Appl. Crystallogr. – volume: 1216 start-page: 7461 year: 2009 end-page: 7465 ident: bb0045 article-title: Size-exclusion chromatography combined with small-angle X-ray scattering optics publication-title: J. Chromatogr. A – volume: 27 start-page: 7924 year: 1998 end-page: 7931 ident: bb0525 article-title: Interparticle interactions and structural changes of nucleosome Core particles in low-salt solution publication-title: Biochemistry – volume: 11 start-page: 462 year: 2004 end-page: 468 ident: bb0020 article-title: Radiation damage to a protein solution, detected by synchrotron X-ray small-angle scattering: dose-related considerations and suppression by cryoprotectants publication-title: J. Synchrotron Radiat. – volume: 6 start-page: 29208 year: 2016 ident: bb0605 article-title: New insight into the dynamical system of αB-crystallin oligomers publication-title: Sci Rep – volume: 106 start-page: 2206 year: 2014 end-page: 2213 ident: bb0530 article-title: Distinct features of the histone core structure in nucleosomes containing the histone H2A.B variant publication-title: Biophys. J. – volume: 20 start-page: 2413 year: 1981 end-page: 2426 ident: bb0495 article-title: Determination of molecular weight by neutron scattering publication-title: Biopolymers – volume: 102 start-page: 1108 year: 2012 end-page: 1117 ident: bb0450 article-title: Functional domain motions in proteins on the ~ publication-title: Biophys. J. – volume: 70 start-page: 177 year: 1970 end-page: 198 ident: bb0110 article-title: Ein Neues Verfahren Zur Bestimmung Der Oberflaechenform Und Der Inneren Struktur von Geloesten Globularen Proteinen Aus Roentgenkleinwinkelmessungen publication-title: Zeitschr. Phys. Chem. Neue Folge. – volume: 36 start-page: 1277 year: 2003 end-page: 1282 ident: bb0620 article-title: PRIMUS: a windows PC-based system for small-angle scattering data analysis publication-title: J. Appl. Crystallogr. – volume: 101 start-page: 2770 year: 2011 end-page: 2781 ident: bb0165 article-title: Improving protein template recognition by using small-angle X-ray scattering profiles publication-title: Biophys. J. – volume: 565 start-page: 3 year: 2015 end-page: 25 ident: bb0565 article-title: Robust high-yield methodologies for 2H and 2H/15N/13C labelling of proteins for structural investigations using neutron scattering and NMR publication-title: Methods Enzymol. – volume: 20 start-page: 542 year: 2011 end-page: 556 ident: bb0355 article-title: The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices publication-title: Protein Sci. – volume: 42 start-page: 15 year: 2017 end-page: 23 ident: bb0360 article-title: Small-angle scattering studies of intrinsically disordered proteins and their complexes publication-title: Curr. Opin. Struct. Biol. – volume: 107 start-page: 435 year: 2014 end-page: 447 ident: bb0195 article-title: Validating solution ensembles from molecular dynamics simulation by wide-angle X-ray scattering data publication-title: Biophys. J. – volume: 89 start-page: 1237 year: 2005 end-page: 1250 ident: bb0210 article-title: Global rigid body modeling of macromolecular complexes against small-angle scattering data publication-title: Biophys. J. – volume: 12 year: 2017 ident: bb0585 article-title: Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering publication-title: Biochem. Biophys. Rep. – volume: 19 start-page: 109 year: 2011 end-page: 116 ident: bb0330 article-title: SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions publication-title: Structure – volume: 94 start-page: 1589 year: 2008 end-page: 1599 ident: bb0245 article-title: Normal-mode flexible fitting of high-resolution structure of biological molecules toward one-dimensional low-resolution data publication-title: Biophys. J. – volume: 19 start-page: 1555 year: 2010 end-page: 1564 ident: bb0350 article-title: Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II? publication-title: Protein Sci. – volume: 7 start-page: 173 year: 1974 end-page: 178 ident: bb0540 article-title: Neutron small-angle scattering of biological macromolecules in solution publication-title: J. Appl. Crystallogr. – volume: 110 start-page: 2037 year: 2011 end-page: 2042 ident: bb0600 article-title: Kinetic asymmetry of subunit exchange of homo-oligomeric protein as revealed by deuteration-assisted small-angle neutron scattering publication-title: Biophys. J. – volume: 281 start-page: 1974 year: 2014 end-page: 1987 ident: bb0260 article-title: Weak protein-ligand interactions studied by small-angle X-ray scattering publication-title: FEBS J. – volume: 108 start-page: 2573 year: 2015 end-page: 2584 ident: bb0255 article-title: Interpretation of solution x-ray scattering by explicit-solvent molecular dynamics publication-title: Biophys. J. – volume: 4 start-page: 28 year: 2015 end-page: 32 ident: bb0535 article-title: Solution structure of variant H2A.Z.1 nucleosome investigated by small-angle X-ray and neutron scatterings publication-title: Biochem. Biophys. Rep. – volume: 500 start-page: 195 year: 2003 end-page: 210 ident: bb0365 article-title: Chemometrics applied to unravel multicomponent processes and mixtures publication-title: Anal. Chim. Acta – volume: 69 start-page: 1997 year: 1972 end-page: 1999 ident: bb0545 article-title: A new method for the determination of biological quarternary structure by neutron scattering publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 79 start-page: 2122 year: 2011 end-page: 2131 ident: bb0345 article-title: Structural memory of natively unfolded tau protein detected by small-angle X-ray scattering publication-title: Proteins – volume: 49 start-page: 13 year: 1986 end-page: 15 ident: bb0560 article-title: Quaternary organization of the 30 S ribosomal subunit of publication-title: Biophys. J. – volume: 70 start-page: 2983 year: 2014 end-page: 2993 ident: bb0570 article-title: Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase publication-title: Acta Crystallogr. Sect. D – volume: 43 start-page: W356 year: 2015 end-page: W361 ident: bb0230 article-title: pyDockSAXS: protein-protein complex structure by SAXS and computational docking publication-title: Nucleic Acids Res. – volume: 18 start-page: 5832 year: 2016 end-page: 5838 ident: bb0340 article-title: Bayesian inference of protein ensembles from SAXS data publication-title: Phys. Chem. Chem. Phys. – volume: 99 start-page: 1329 year: 2002 end-page: 1334 ident: bb0400 article-title: Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 94 start-page: 4906 year: 2008 end-page: 4923 ident: bb0375 article-title: Analysis of self-associating proteins by singular value decomposition of solution scattering data publication-title: Biophys. J. – volume: 174 start-page: 265 year: 1984 end-page: 284 ident: bb0555 article-title: Positions of proteins S14, S18 and S20 in the 30 S ribosomal subunit of publication-title: J. Mol. Biol. – volume: 39 start-page: 911 year: 1976 end-page: 953 ident: bb0490 article-title: The study of biological structures by neutron scattering from solution publication-title: Rep. Prog. Phys. – volume: 23 start-page: 748 year: 2013 end-page: 754 ident: bb0005 article-title: Impact and progress in small and wide angle X-ray scattering (SAXS and WAXS) publication-title: Curr. Opin. Struct. Biol. – ident: bb0475 – reference: You can get a visual image from – volume: 39 start-page: 769 year: 2010 end-page: 780 ident: bb0240 article-title: Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering publication-title: Eur. Biophys. J. – volume: 11 start-page: 2122 year: 2016 end-page: 2153 ident: bb0080 article-title: Preparing monodisperse macromolecular samples for successful biological small-angle X-ray and neutron-scattering experiments publication-title: Nat. Protoc. – volume: 52 start-page: 419 year: 1996 end-page: 426 ident: bb0115 article-title: New developments in direct shape determination from small-angle scattering. 2. Uniqueness publication-title: Acta Crystallogr. Sect. A: Found. Crystallogr. – volume: 19 start-page: 229 year: 1986 end-page: 242 ident: bb0460 publication-title: J. Appl. Crystallogr. – volume: 8 start-page: 151 year: 2012 end-page: 167 ident: bb0290 article-title: Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering publication-title: Mol. BioSyst. – volume: 116 start-page: 6424 year: 2016 end-page: 6462 ident: bb0285 article-title: Dynamic protein interaction networks and new structural paradigms in signaling publication-title: Chem. Rev. – volume: 24 start-page: 63 year: 2017 end-page: 72 ident: bb0030 article-title: Development of tools to automate quantitative analysis of radiation damage in SAXS experiments publication-title: J. Synchrotron Radiat. – volume: 870 start-page: 261 year: 2015 end-page: 289 ident: bb0300 article-title: Application of SAXS for the structural characterization of IDPs publication-title: Adv. Exp. Med. Biol. – volume: F67 start-page: 336 year: 2011 end-page: 339 ident: bb0050 article-title: Purification, crystallization, small-angle X-ray scattering and preliminary X-ray diffraction analysis of the SH2 domain of the Csk-homologous kinase publication-title: Acta Cryst – ident: bb0430 – volume: 261 start-page: 658 year: 1996 end-page: 671 ident: bb0385 article-title: A lysozyme folding intermediate revealed by solution X-ray scattering publication-title: J. Mol. Biol. – volume: 11 start-page: 429 year: 2010 ident: bb0155 article-title: Calculation of accurate small angle X-ray scattering curves from coarse-grained protein models publication-title: BMC Bioinf. – volume: 133 start-page: 393 year: 1983 end-page: 398 ident: bb0520 article-title: Neutron-scattering studies of accurately reconstituted nucleosome core particles and the effect of ionic strength on core particle structure publication-title: Eur. J. Biochem. – volume: 39 start-page: W184 year: 2011 end-page: W189 ident: bb0175 article-title: AquaSAXS: a web server for computation and fitting of SAXS profiles with non-uniformally hydrated atomic models publication-title: Nucleic Acids Res. – volume: 30 start-page: 280 year: 1997 end-page: 293 ident: bb0470 publication-title: J. Appl. Crystallogr. – volume: 308 start-page: 721 year: 2001 end-page: 743 ident: bb0395 article-title: Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering publication-title: J. Mol. Biol. – volume: 25 start-page: 5 year: 2017 end-page: 15 ident: bb0405 article-title: Structural analysis of multi-component amyloid systems by chemometric SAXS data decomposition publication-title: Structure – volume: 11 start-page: 314 year: 2004 end-page: 318 ident: bb0035 article-title: Liquid-chromatography-coupled SAXS for accurate sizing of aggregating proteins publication-title: J. Synchrotron Radiat. – volume: 11 year: 2016 ident: bb0065 article-title: Structure of a bacterial virus DNA-injection protein complex reveals a decameric assembly with a constricted molecular channel publication-title: PLoS One – volume: 153 start-page: 761 year: 1981 end-page: 780 ident: bb0550 article-title: Position of protein Sl in the 30 S ribosomal subunit of publication-title: J. Mol. Biol. – volume: 4 start-page: 3769 year: 1977 end-page: 3786 ident: bb0515 article-title: A low resolution model for the chromatin core particle by neutron scattering publication-title: Nucleic Acids Res. – volume: 44 start-page: 1264 year: 2011 end-page: 1271 ident: bb0235 article-title: J, DADIMODO: a program for refining the structure of multidomain proteins and complexes against small-angle scattering data and NMR-derived restraints publication-title: J. Appl. Crystallogr. – volume: 49 start-page: 1827 year: 2016 end-page: 1841 ident: bb0095 article-title: US-SOMO HPLC-SAXS module: dealing with capillary fouling and extraction of pure component patterns from poorly resolved SEC-SAXS data publication-title: J. Appl. Crystallogr. – volume: 107 start-page: 15757 year: 2010 end-page: 15762 ident: bb0320 article-title: Multidomain assembled states of Hck tyrosine kinase in solution publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 30 start-page: 1140 year: 1997 end-page: 1147 ident: bb0465 article-title: SANS at Pulsed Neutron Sources: Present & future prospects publication-title: J. Appl. Crystallogr. – volume: 49 start-page: 2015 year: 2016 end-page: 2020 ident: bb0625 article-title: SEC-SANS: size exclusion chromatography combined in situ with small-angle neutron scattering publication-title: J. Appl. Crystallogr. – volume: 42 start-page: 892 year: 2009 end-page: 900 ident: bb0040 article-title: Combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments at the synchrotron SOLEIL SWING beamline publication-title: J. Appl. Crystallogr. – volume: 70 start-page: 17.14.1 year: 2012 end-page: 17.14.18 ident: bb0025 article-title: Sample preparation, data collection, and preliminary data analysis in biomolecular solution X-ray scattering publication-title: Curr. Protoc. Protein Sci. – volume: 68 start-page: 278 year: 2012 end-page: 285 ident: bb0170 article-title: Computation of small-angle scattering profiles with three-dimensional Zernike polynomials publication-title: Acta Crystallogr. Sect. A: Found. Crystallogr. – volume: 44 start-page: 1411 year: 2016 end-page: 1420 ident: bb0060 article-title: Binding of transcription factor GabR to DNA requires recognition of DNA shape at a location distinct from its cognate binding site publication-title: Nucleic Acids Res. – volume: 28 start-page: 768 year: 1995 end-page: 773 ident: bb0150 article-title: CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates publication-title: J. Appl. Crystallogr. – volume: 74 start-page: 2760 year: 1998 end-page: 2775 ident: bb0120 article-title: Low-resolution structures of proteins in solution retrieved from X-ray scattering with a genetic algorithm publication-title: Biophys. J. – volume: 99 start-page: 2309 year: 2010 end-page: 2317 ident: bb0445 article-title: Large domain fluctuations on 50-ns timescale enable catalytic activity in phosphoglycerate kinase publication-title: Biophys. J. – year: 1987 ident: bb0480 article-title: Structure Analysis by Small-angle X-ray and Neutron Scattering – volume: 28 start-page: 174 year: 2009 end-page: 189 ident: bb0315 article-title: Structure and flexibility within proteins as identified through small angle X-ray scattering publication-title: Gen. Physiol. Biophys. – volume: 132 start-page: 13553 year: 2010 end-page: 13558 ident: bb0325 article-title: Conformational space of flexible biological macromolecules from average data publication-title: J. Am. Chem. Soc. – reference: I. N. Serdyuk, N. R. Zaccai, J. Zaccai, Methods in Molecular Biophysics: Structure, Dynamics, Function, Cambridge University Press. – volume: 105 start-page: 18360 year: 2008 end-page: 18365 ident: bb0595 article-title: Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function publication-title: PNAS – reference: P. Lindner, R. P. May, P. A. Timmins, Upgrading of the SANS instrument D11 at the ILL, Physica B, 180–181 (1992) 967–972. – volume: 45 start-page: 342 year: 2012 end-page: 350 ident: bb0090 article-title: New developments in the ATSAS program package for small-angle scattering data analysis publication-title: J. Appl. Crystallogr. – volume: 37 start-page: 12443 year: 1998 end-page: 12451 ident: bb0390 article-title: Protein denaturation: a small-angle X-ray scattering study of the ensemble of unfolded states of cytochrome c publication-title: Biochemist – volume: 22 start-page: 670 year: 2012 end-page: 678 ident: bb0055 article-title: Advances in X-ray scattering: from solution SAXS to achievements with coherent beams publication-title: Curr. Opin. Struct. Biol. – volume: 2 start-page: 207 year: 2015 end-page: 217 ident: bb0310 article-title: Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering publication-title: IUCrJ – volume: 47 start-page: 430 year: 2014 end-page: 435 ident: bb0575 article-title: Conformational characterization of a protein complex involving intrinsically disordered protein by small-angle neutron scattering using the inverse contrast matching method: a case study of interaction between α-synuclein and PbaB tetramer as a model chaperone publication-title: J. Appl. Crystallogr. – volume: 76 start-page: 2879 year: 1999 end-page: 2886 ident: bb0125 article-title: Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing publication-title: Biophys. J. – volume: 129 start-page: 5656 year: 2007 end-page: 5664 ident: bb0305 article-title: Structural characterization of flexible proteins using small-angle X-ray scattering publication-title: J. Am. Chem. Soc. – volume: 42 start-page: 342 year: 2009 end-page: 346 ident: bb0130 article-title: DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering publication-title: J. Appl. Crystallogr. – volume: 104 start-page: 873 year: 2013 end-page: 883 ident: bb0410 article-title: Wide-angle X-ray solution scattering for protein-ligand binding: multivariate curve resolution with Bayesian confidence intervals publication-title: Biophys. J. – volume: 134 start-page: 10080 year: 2012 end-page: 10088 ident: bb0070 article-title: Modeling detergent organization around aquaporin-0 using small-angle X-ray scattering publication-title: J. Am. Chem. Soc. – volume: 40 start-page: 1 year: 2016 end-page: 7 ident: bb0015 article-title: Small-angle scattering and 3D structure interpretation publication-title: Curr. Opin. Struct. Biol. – volume: 6 start-page: 38399 year: 2016 ident: bb0485 article-title: A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion publication-title: Sci Rep – reference: . – volume: 255 start-page: 146 year: 1972 ident: bb0440 article-title: Neutron Spin Echo; a new concept in polarized thermal neutron techniques publication-title: Z. Phys. – volume: 355 start-page: 1174 year: 2017 end-page: 1180 ident: bb0590 article-title: Structural basis of the day-night transition in a bacterial circadian clock publication-title: Science – volume: 137 start-page: 15122 year: 2015 end-page: 15134 ident: bb0280 article-title: Large-scale conformational dynamics control H5N1 influenza polymerase PB2 binding to importin α publication-title: J. Am. Chem. Soc. – volume: 98 start-page: 238101 year: 2007 ident: bb0610 article-title: Determination of interbilayer and transbilayer lipid transfers by time-resolved small-angle neutron scattering publication-title: Phys. Rev. Lett. – volume: 36 start-page: 860 year: 2003 end-page: 864 ident: bb0135 article-title: Uniqueness of ab initio shape determination in small-angle scattering publication-title: J. Appl. Crystallogr. – volume: 173 start-page: 461 year: 2011 end-page: 471 ident: bb0215 article-title: Macromolecular docking restrained by a small angle X-ray scattering profile publication-title: J. Struct. Biol. – volume: 44 start-page: W424 year: 2016 end-page: W429 ident: bb0220 article-title: FoXS, FoXSDock and MultiFoXS: single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles publication-title: Nucleic Acids Res. – volume: 3 start-page: 440 year: 2016 end-page: 447 ident: bb0145 article-title: Resolution of ab initio shapes determined from small-angle scattering publication-title: IUCrJ. – volume: 6 start-page: 30287 year: 2016 ident: bb0505 article-title: Self-assembly controls self-cleavage of HHR from ASBVd(−): a combined SANS and modeling study publication-title: Sci Rep – volume: 43 start-page: W225 year: 2015 end-page: W230 ident: bb0200 article-title: WAXSiS: a web server for the calculation of SAXS/WAXS curves based on explicit-solvent molecular dynamics publication-title: Nucleic Acids Res. – volume: 39 start-page: W184 year: 2011 ident: 10.1016/j.bbagen.2017.10.015_bb0175 article-title: AquaSAXS: a web server for computation and fitting of SAXS profiles with non-uniformally hydrated atomic models publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkr430 – volume: 11 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0065 article-title: Structure of a bacterial virus DNA-injection protein complex reveals a decameric assembly with a constricted molecular channel publication-title: PLoS One – volume: 101 start-page: 2770 year: 2011 ident: 10.1016/j.bbagen.2017.10.015_bb0165 article-title: Improving protein template recognition by using small-angle X-ray scattering profiles publication-title: Biophys. J. doi: 10.1016/j.bpj.2011.10.046 – volume: 45 start-page: 342 year: 2012 ident: 10.1016/j.bbagen.2017.10.015_bb0090 article-title: New developments in the ATSAS program package for small-angle scattering data analysis publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889812007662 – volume: F67 start-page: 336 year: 2011 ident: 10.1016/j.bbagen.2017.10.015_bb0050 article-title: Purification, crystallization, small-angle X-ray scattering and preliminary X-ray diffraction analysis of the SH2 domain of the Csk-homologous kinase publication-title: Acta Cryst – volume: 11 start-page: 429 year: 2010 ident: 10.1016/j.bbagen.2017.10.015_bb0155 article-title: Calculation of accurate small angle X-ray scattering curves from coarse-grained protein models publication-title: BMC Bioinf. doi: 10.1186/1471-2105-11-429 – volume: 131 start-page: 4378 year: 2009 ident: 10.1016/j.bbagen.2017.10.015_bb0380 article-title: Low-resolution structures of transient protein-protein complexes using small-angle X-ray scattering publication-title: J. Am. Chem. Soc. doi: 10.1021/ja808490b – volume: 44 start-page: 1411 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0060 article-title: Binding of transcription factor GabR to DNA requires recognition of DNA shape at a location distinct from its cognate binding site publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv1466 – volume: 102 start-page: 1108 issue: 5 year: 2012 ident: 10.1016/j.bbagen.2017.10.015_bb0450 article-title: Functional domain motions in proteins on the ~1–100ns timescale: comparison of neutron spin-echo spectroscopy of phosphoglycerate kinase with molecular-dynamics simulation publication-title: Biophys. J. doi: 10.1016/j.bpj.2012.01.002 – volume: 1216 start-page: 7461 year: 2009 ident: 10.1016/j.bbagen.2017.10.015_bb0045 article-title: Size-exclusion chromatography combined with small-angle X-ray scattering optics publication-title: J. Chromatogr. A doi: 10.1016/j.chroma.2009.02.053 – volume: 39 start-page: 769 year: 2010 ident: 10.1016/j.bbagen.2017.10.015_bb0240 article-title: Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering publication-title: Eur. Biophys. J. doi: 10.1007/s00249-009-0549-3 – volume: 25 start-page: 5 year: 2017 ident: 10.1016/j.bbagen.2017.10.015_bb0405 article-title: Structural analysis of multi-component amyloid systems by chemometric SAXS data decomposition publication-title: Structure doi: 10.1016/j.str.2016.10.013 – volume: 18 start-page: 716 year: 2009 ident: 10.1016/j.bbagen.2017.10.015_bb0270 article-title: Structural characterization of unphosphorylated STAT5a oligomerization equilibrium in solution by small-angle X-ray scattering publication-title: Protein Sci. doi: 10.1002/pro.83 – volume: 6 start-page: 38399 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0485 article-title: A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion publication-title: Sci Rep doi: 10.1038/srep38399 – volume: 28 start-page: 768 year: 1995 ident: 10.1016/j.bbagen.2017.10.015_bb0150 article-title: CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889895007047 – volume: 428 start-page: 1197 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0075 article-title: Novel helical assembly in arginine methyltransferase 8 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2016.02.007 – volume: 6 start-page: 35567 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0580 article-title: Structural characterization of the circadian clock protein complex composed of KaiB and KaiC by inverse contrast-matching small-angle neutron scattering publication-title: Sci Rep doi: 10.1038/srep35567 – volume: 70 start-page: 177 year: 1970 ident: 10.1016/j.bbagen.2017.10.015_bb0110 article-title: Ein Neues Verfahren Zur Bestimmung Der Oberflaechenform Und Der Inneren Struktur von Geloesten Globularen Proteinen Aus Roentgenkleinwinkelmessungen publication-title: Zeitschr. Phys. Chem. Neue Folge. doi: 10.1524/zpch.1970.72.4_6.177 – volume: 137 start-page: 15122 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0280 article-title: Large-scale conformational dynamics control H5N1 influenza polymerase PB2 binding to importin α publication-title: J. Am. Chem. Soc. doi: 10.1021/jacs.5b07765 – volume: 79 start-page: 2122 year: 2011 ident: 10.1016/j.bbagen.2017.10.015_bb0345 article-title: Structural memory of natively unfolded tau protein detected by small-angle X-ray scattering publication-title: Proteins doi: 10.1002/prot.23033 – volume: 12 year: 2017 ident: 10.1016/j.bbagen.2017.10.015_bb0585 article-title: Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering publication-title: Biochem. Biophys. Rep. – volume: 6 start-page: 30287 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0505 article-title: Self-assembly controls self-cleavage of HHR from ASBVd(−): a combined SANS and modeling study publication-title: Sci Rep doi: 10.1038/srep30287 – volume: 76 start-page: 2879 year: 1999 ident: 10.1016/j.bbagen.2017.10.015_bb0125 article-title: Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing publication-title: Biophys. J. doi: 10.1016/S0006-3495(99)77443-6 – volume: 20 start-page: 542 year: 2011 ident: 10.1016/j.bbagen.2017.10.015_bb0355 article-title: The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices publication-title: Protein Sci. doi: 10.1002/pro.587 – volume: 19 start-page: 229 year: 1986 ident: 10.1016/j.bbagen.2017.10.015_bb0460 publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889886089513 – volume: 23 start-page: 748 year: 2013 ident: 10.1016/j.bbagen.2017.10.015_bb0005 article-title: Impact and progress in small and wide angle X-ray scattering (SAXS and WAXS) publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2013.06.007 – volume: 19 start-page: 109 year: 2011 ident: 10.1016/j.bbagen.2017.10.015_bb0330 article-title: SAXS ensemble refinement of ESCRT-III CHMP3 conformational transitions publication-title: Structure doi: 10.1016/j.str.2010.10.006 – volume: 132 start-page: 13553 year: 2010 ident: 10.1016/j.bbagen.2017.10.015_bb0325 article-title: Conformational space of flexible biological macromolecules from average data publication-title: J. Am. Chem. Soc. doi: 10.1021/ja1063923 – volume: 19 start-page: 1555 year: 2010 ident: 10.1016/j.bbagen.2017.10.015_bb0350 article-title: Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II? publication-title: Protein Sci. doi: 10.1002/pro.435 – volume: 20 start-page: 2413 year: 1981 ident: 10.1016/j.bbagen.2017.10.015_bb0495 article-title: Determination of molecular weight by neutron scattering publication-title: Biopolymers doi: 10.1002/bip.1981.360201110 – volume: 45 start-page: 342 year: 2012 ident: 10.1016/j.bbagen.2017.10.015_bb0265 article-title: New developments in the ATSAS program package for small-angle scattering data analysis publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889812007662 – volume: 110 start-page: 2037 issue: 8 year: 2011 ident: 10.1016/j.bbagen.2017.10.015_bb0600 article-title: Kinetic asymmetry of subunit exchange of homo-oligomeric protein as revealed by deuteration-assisted small-angle neutron scattering publication-title: Biophys. J. doi: 10.1016/j.bpj.2011.09.004 – volume: 38 start-page: W540 year: 2010 ident: 10.1016/j.bbagen.2017.10.015_bb0185 article-title: FoXS: a web server for rapid computation and fitting of SAXS profiles publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkq461 – volume: 355 start-page: 1174 year: 2017 ident: 10.1016/j.bbagen.2017.10.015_bb0590 article-title: Structural basis of the day-night transition in a bacterial circadian clock publication-title: Science doi: 10.1126/science.aag2516 – volume: 49 start-page: 1827 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0095 article-title: US-SOMO HPLC-SAXS module: dealing with capillary fouling and extraction of pure component patterns from poorly resolved SEC-SAXS data publication-title: J. Appl. Crystallogr. doi: 10.1107/S1600576716011201 – volume: 116 start-page: 6424 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0285 article-title: Dynamic protein interaction networks and new structural paradigms in signaling publication-title: Chem. Rev. doi: 10.1021/acs.chemrev.5b00548 – ident: 10.1016/j.bbagen.2017.10.015_bb0455 – volume: 133 start-page: 393 year: 1983 ident: 10.1016/j.bbagen.2017.10.015_bb0520 article-title: Neutron-scattering studies of accurately reconstituted nucleosome core particles and the effect of ionic strength on core particle structure publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1983.tb07475.x – volume: 94 start-page: 4906 year: 2008 ident: 10.1016/j.bbagen.2017.10.015_bb0375 article-title: Analysis of self-associating proteins by singular value decomposition of solution scattering data publication-title: Biophys. J. doi: 10.1529/biophysj.107.113167 – volume: 153 start-page: 761 year: 1981 ident: 10.1016/j.bbagen.2017.10.015_bb0550 article-title: Position of protein Sl in the 30 S ribosomal subunit of Escherichia coli publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(81)90417-4 – volume: 44 start-page: W424 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0220 article-title: FoXS, FoXSDock and MultiFoXS: single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkw389 – volume: 40 start-page: 1 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0015 article-title: Small-angle scattering and 3D structure interpretation publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2016.05.003 – volume: 49 start-page: 2015 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0625 article-title: SEC-SANS: size exclusion chromatography combined in situ with small-angle neutron scattering publication-title: J. Appl. Crystallogr. doi: 10.1107/S1600576716016514 – volume: 8 start-page: 151 year: 2012 ident: 10.1016/j.bbagen.2017.10.015_bb0290 article-title: Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering publication-title: Mol. BioSyst. doi: 10.1039/C1MB05275F – year: 1987 ident: 10.1016/j.bbagen.2017.10.015_bb0480 – volume: 70 start-page: 17.14.1 year: 2012 ident: 10.1016/j.bbagen.2017.10.015_bb0025 article-title: Sample preparation, data collection, and preliminary data analysis in biomolecular solution X-ray scattering publication-title: Curr. Protoc. Protein Sci. doi: 10.1002/0471140864.ps1714s70 – volume: 43 start-page: W356 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0230 article-title: pyDockSAXS: protein-protein complex structure by SAXS and computational docking publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv368 – volume: 99 start-page: 1329 year: 2002 ident: 10.1016/j.bbagen.2017.10.015_bb0400 article-title: Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle x-ray scattering publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.012458999 – volume: 8 start-page: 1 year: 2013 ident: 10.1016/j.bbagen.2017.10.015_bb0190 article-title: Reconstruction of Saxs profiles from protein structures publication-title: Comput. Struct. Biotechnol. J. doi: 10.5936/csbj.201308006 – volume: 94 start-page: 1589 year: 2008 ident: 10.1016/j.bbagen.2017.10.015_bb0245 article-title: Normal-mode flexible fitting of high-resolution structure of biological molecules toward one-dimensional low-resolution data publication-title: Biophys. J. doi: 10.1529/biophysj.107.122218 – volume: 105 start-page: 962 year: 2013 ident: 10.1016/j.bbagen.2017.10.015_bb0180 article-title: Accurate SAXS profile computation and its assessment by contrast variation experiments publication-title: Biophys. J. doi: 10.1016/j.bpj.2013.07.020 – volume: 89 start-page: 1237 year: 2005 ident: 10.1016/j.bbagen.2017.10.015_bb0210 article-title: Global rigid body modeling of macromolecular complexes against small-angle scattering data publication-title: Biophys. J. doi: 10.1529/biophysj.105.064154 – volume: 70 start-page: 2983 year: 2014 ident: 10.1016/j.bbagen.2017.10.015_bb0570 article-title: Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase publication-title: Acta Crystallogr. Sect. D doi: 10.1107/S1399004714018446 – volume: 24 start-page: 63 year: 2017 ident: 10.1016/j.bbagen.2017.10.015_bb0030 article-title: Development of tools to automate quantitative analysis of radiation damage in SAXS experiments publication-title: J. Synchrotron Radiat. doi: 10.1107/S1600577516015083 – volume: 43 start-page: W225 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0200 article-title: WAXSiS: a web server for the calculation of SAXS/WAXS curves based on explicit-solvent molecular dynamics publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv309 – volume: 106 start-page: 2206 year: 2014 ident: 10.1016/j.bbagen.2017.10.015_bb0530 article-title: Distinct features of the histone core structure in nucleosomes containing the histone H2A.B variant publication-title: Biophys. J. doi: 10.1016/j.bpj.2014.04.007 – volume: 565 start-page: 3 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0565 article-title: Robust high-yield methodologies for 2H and 2H/15N/13C labelling of proteins for structural investigations using neutron scattering and NMR publication-title: Methods Enzymol. doi: 10.1016/bs.mie.2015.06.014 – volume: 7 start-page: 173 year: 1974 ident: 10.1016/j.bbagen.2017.10.015_bb0540 article-title: Neutron small-angle scattering of biological macromolecules in solution publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889874009071 – volume: 68 start-page: 278 year: 2012 ident: 10.1016/j.bbagen.2017.10.015_bb0170 article-title: Computation of small-angle scattering profiles with three-dimensional Zernike polynomials publication-title: Acta Crystallogr. Sect. A: Found. Crystallogr. doi: 10.1107/S010876731104788X – volume: 107 start-page: 435 year: 2014 ident: 10.1016/j.bbagen.2017.10.015_bb0195 article-title: Validating solution ensembles from molecular dynamics simulation by wide-angle X-ray scattering data publication-title: Biophys. J. doi: 10.1016/j.bpj.2014.06.006 – volume: 281 start-page: 1974 year: 2014 ident: 10.1016/j.bbagen.2017.10.015_bb0260 article-title: Weak protein-ligand interactions studied by small-angle X-ray scattering publication-title: FEBS J. doi: 10.1111/febs.12772 – volume: 129 start-page: 5656 year: 2007 ident: 10.1016/j.bbagen.2017.10.015_bb0305 article-title: Structural characterization of flexible proteins using small-angle X-ray scattering publication-title: J. Am. Chem. Soc. doi: 10.1021/ja069124n – volume: 6 start-page: 5116 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0275 article-title: Structural properties of protein-detergent complexes from SAXS and MD simulations publication-title: J. Phys. Chem. Lett. doi: 10.1021/acs.jpclett.5b02399 – volume: 29 start-page: 703 year: 2008 ident: 10.1016/j.bbagen.2017.10.015_bb0415 article-title: Assembly and disassembly dynamics of the cyanobacterial periodosome publication-title: Mol. Cell doi: 10.1016/j.molcel.2008.01.015 – volume: 105 start-page: 18360 year: 2008 ident: 10.1016/j.bbagen.2017.10.015_bb0595 article-title: Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function publication-title: PNAS doi: 10.1073/pnas.0808903105 – volume: 42 start-page: 342 year: 2009 ident: 10.1016/j.bbagen.2017.10.015_bb0130 article-title: DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889809000338 – volume: 39 start-page: 911 year: 1976 ident: 10.1016/j.bbagen.2017.10.015_bb0490 article-title: The study of biological structures by neutron scattering from solution publication-title: Rep. Prog. Phys. doi: 10.1088/0034-4885/39/10/001 – volume: 7 start-page: 40948 year: 2017 ident: 10.1016/j.bbagen.2017.10.015_bb0615 article-title: Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase publication-title: Sci Rep doi: 10.1038/srep40948 – volume: 22 start-page: 670 year: 2012 ident: 10.1016/j.bbagen.2017.10.015_bb0055 article-title: Advances in X-ray scattering: from solution SAXS to achievements with coherent beams publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2012.07.014 – volume: 69 start-page: 1997 year: 1972 ident: 10.1016/j.bbagen.2017.10.015_bb0545 article-title: A new method for the determination of biological quarternary structure by neutron scattering publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.69.8.1997 – volume: 47 start-page: 1501 year: 2017 ident: 10.1016/j.bbagen.2017.10.015_bb0205 article-title: Disentangling polydispersity in the PCNA-p15PAF complex, a disordered, transient and multivalent macromolecular assembly publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkw1183 – ident: 10.1016/j.bbagen.2017.10.015_bb0420 – volume: 44 start-page: 1264 year: 2011 ident: 10.1016/j.bbagen.2017.10.015_bb0235 article-title: J, DADIMODO: a program for refining the structure of multidomain proteins and complexes against small-angle scattering data and NMR-derived restraints publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889811035758 – volume: 2 start-page: 2163 year: 1975 ident: 10.1016/j.bbagen.2017.10.015_bb0510 article-title: Low-angle neutron scattering from chromatin subunit particles publication-title: Nucleic Acids Res. doi: 10.1093/nar/2.11.2163 – volume: 4 start-page: 3769 year: 1977 ident: 10.1016/j.bbagen.2017.10.015_bb0515 article-title: A low resolution model for the chromatin core particle by neutron scattering publication-title: Nucleic Acids Res. doi: 10.1093/nar/4.11.3769 – volume: 255 start-page: 146 year: 1972 ident: 10.1016/j.bbagen.2017.10.015_bb0440 article-title: Neutron Spin Echo; a new concept in polarized thermal neutron techniques publication-title: Z. Phys. doi: 10.1007/BF01394523 – volume: 132 start-page: 15484 year: 2010 ident: 10.1016/j.bbagen.2017.10.015_bb0160 article-title: Improved fitting of solution X-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling publication-title: J. Am. Chem. Soc. doi: 10.1021/ja106173n – volume: 36 start-page: 860 year: 2003 ident: 10.1016/j.bbagen.2017.10.015_bb0135 article-title: Uniqueness of ab initio shape determination in small-angle scattering publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889803000268 – volume: 48 start-page: 1102 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0100 article-title: Methods for analysis of size-exclusion chromatography–small-angle X-ray scattering and reconstruction of protein scattering publication-title: J. Appl. Crystallogr. doi: 10.1107/S1600576715010420 – volume: 870 start-page: 261 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0300 article-title: Application of SAXS for the structural characterization of IDPs publication-title: Adv. Exp. Med. Biol. doi: 10.1007/978-3-319-20164-1_8 – volume: 11 start-page: 462 year: 2004 ident: 10.1016/j.bbagen.2017.10.015_bb0020 article-title: Radiation damage to a protein solution, detected by synchrotron X-ray small-angle scattering: dose-related considerations and suppression by cryoprotectants publication-title: J. Synchrotron Radiat. doi: 10.1107/S0909049504019272 – volume: 74 start-page: 2760 year: 1998 ident: 10.1016/j.bbagen.2017.10.015_bb0120 article-title: Low-resolution structures of proteins in solution retrieved from X-ray scattering with a genetic algorithm publication-title: Biophys. J. doi: 10.1016/S0006-3495(98)77984-6 – volume: 108 start-page: 2573 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0255 article-title: Interpretation of solution x-ray scattering by explicit-solvent molecular dynamics publication-title: Biophys. J. doi: 10.1016/j.bpj.2015.03.062 – volume: 99 start-page: 2309 issue: 7 year: 2010 ident: 10.1016/j.bbagen.2017.10.015_bb0445 article-title: Large domain fluctuations on 50-ns timescale enable catalytic activity in phosphoglycerate kinase publication-title: Biophys. J. doi: 10.1016/j.bpj.2010.08.017 – volume: 98 start-page: 238101 issue: 23 year: 2007 ident: 10.1016/j.bbagen.2017.10.015_bb0610 article-title: Determination of interbilayer and transbilayer lipid transfers by time-resolved small-angle neutron scattering publication-title: Phys. Rev. Lett. doi: 10.1103/PhysRevLett.98.238101 – volume: 30 start-page: 280 year: 1997 ident: 10.1016/j.bbagen.2017.10.015_bb0470 publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889896013398 – volume: 42 start-page: 892 year: 2009 ident: 10.1016/j.bbagen.2017.10.015_bb0040 article-title: Combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments at the synchrotron SOLEIL SWING beamline publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889809029288 – volume: 18 start-page: 5832 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0340 article-title: Bayesian inference of protein ensembles from SAXS data publication-title: Phys. Chem. Chem. Phys. doi: 10.1039/C5CP04886A – volume: 6 start-page: 29208 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0605 article-title: New insight into the dynamical system of αB-crystallin oligomers publication-title: Sci Rep doi: 10.1038/srep29208 – volume: 500 start-page: 195 year: 2003 ident: 10.1016/j.bbagen.2017.10.015_bb0365 article-title: Chemometrics applied to unravel multicomponent processes and mixtures publication-title: Anal. Chim. Acta doi: 10.1016/S0003-2670(03)00724-4 – volume: 6 start-page: 469 year: 2007 ident: 10.1016/j.bbagen.2017.10.015_bb0370 article-title: Chemometrics in metabonomics publication-title: J. Proteome Res. doi: 10.1021/pr060594q – year: 2005 ident: 10.1016/j.bbagen.2017.10.015_bb0435 article-title: Neutron Scattering from Magnetic Materials 1st Edition – volume: 126 start-page: 293 year: 1978 ident: 10.1016/j.bbagen.2017.10.015_bb0500 article-title: Antico-operative binding of initiator transfer RNAMet to methionyl-transfer RNA synthetase from Escherichia coli: neutron scattering studies publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(78)90042-6 – volume: 52 start-page: 419 year: 1996 ident: 10.1016/j.bbagen.2017.10.015_bb0115 article-title: New developments in direct shape determination from small-angle scattering. 2. Uniqueness publication-title: Acta Crystallogr. Sect. A: Found. Crystallogr. doi: 10.1107/S0108767396000177 – volume: 8 start-page: 308 year: 2012 ident: 10.1016/j.bbagen.2017.10.015_bb0335 article-title: Understanding the structural ensembles of a highly extended disordered protein publication-title: Mol. BioSyst. doi: 10.1039/C1MB05243H – volume: 107 start-page: 15757 year: 2010 ident: 10.1016/j.bbagen.2017.10.015_bb0320 article-title: Multidomain assembled states of Hck tyrosine kinase in solution publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1004569107 – volume: 36 start-page: 1277 year: 2003 ident: 10.1016/j.bbagen.2017.10.015_bb0620 article-title: PRIMUS: a windows PC-based system for small-angle scattering data analysis publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889803012779 – volume: 28 start-page: 174 year: 2009 ident: 10.1016/j.bbagen.2017.10.015_bb0315 article-title: Structure and flexibility within proteins as identified through small angle X-ray scattering publication-title: Gen. Physiol. Biophys. doi: 10.4149/gpb_2009_02_174 – volume: 173 start-page: 461 year: 2011 ident: 10.1016/j.bbagen.2017.10.015_bb0215 article-title: Macromolecular docking restrained by a small angle X-ray scattering profile publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2010.09.023 – volume: 30 start-page: 1140 year: 1997 ident: 10.1016/j.bbagen.2017.10.015_bb0465 article-title: SANS at Pulsed Neutron Sources: Present & future prospects publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889897002173 – volume: 134 start-page: 10080 year: 2012 ident: 10.1016/j.bbagen.2017.10.015_bb0070 article-title: Modeling detergent organization around aquaporin-0 using small-angle X-ray scattering publication-title: J. Am. Chem. Soc. doi: 10.1021/ja301667n – volume: 2 start-page: 207 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0310 article-title: Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering publication-title: IUCrJ doi: 10.1107/S205225251500202X – volume: 42 start-page: 15 year: 2017 ident: 10.1016/j.bbagen.2017.10.015_bb0360 article-title: Small-angle scattering studies of intrinsically disordered proteins and their complexes publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2016.10.011 – ident: 10.1016/j.bbagen.2017.10.015_bb0105 – volume: 308 start-page: 721 year: 2001 ident: 10.1016/j.bbagen.2017.10.015_bb0395 article-title: Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2001.4611 – volume: 403 start-page: 217 year: 2010 ident: 10.1016/j.bbagen.2017.10.015_bb0225 article-title: Structural characterization of protein-protein complexes by integrating computational docking with small-angle scattering data publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2010.08.029 – volume: 174 start-page: 265 year: 1984 ident: 10.1016/j.bbagen.2017.10.015_bb0555 article-title: Positions of proteins S14, S18 and S20 in the 30 S ribosomal subunit of Escherichia coli publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(84)90338-3 – volume: 47 start-page: 430 year: 2014 ident: 10.1016/j.bbagen.2017.10.015_bb0575 publication-title: J. Appl. Crystallogr. doi: 10.1107/S1600576713033475 – volume: 3 start-page: 440 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0145 article-title: Resolution of ab initio shapes determined from small-angle scattering publication-title: IUCrJ. doi: 10.1107/S2052252516016018 – ident: 10.1016/j.bbagen.2017.10.015_bb0425 doi: 10.1016/0921-4526(92)90524-V – volume: 4 start-page: 28 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0535 article-title: Solution structure of variant H2A.Z.1 nucleosome investigated by small-angle X-ray and neutron scatterings publication-title: Biochem. Biophys. Rep. – volume: 11 start-page: 2122 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0080 article-title: Preparing monodisperse macromolecular samples for successful biological small-angle X-ray and neutron-scattering experiments publication-title: Nat. Protoc. doi: 10.1038/nprot.2016.113 – volume: 261 start-page: 658 year: 1996 ident: 10.1016/j.bbagen.2017.10.015_bb0385 article-title: A lysozyme folding intermediate revealed by solution X-ray scattering publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1996.0491 – volume: 1741 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0085 article-title: Software development for analysis of small-angle X-ray scattering data publication-title: AIP Conf. Proc. doi: 10.1063/1.4952937 – volume: 40 start-page: 191 year: 2007 ident: 10.1016/j.bbagen.2017.10.015_bb0010 article-title: X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution publication-title: Q. Rev. Biophys. doi: 10.1017/S0033583507004635 – volume: 13 start-page: 55 year: 2012 ident: 10.1016/j.bbagen.2017.10.015_bb0295 article-title: How random are intrinsically disordered proteins? A small angle scattering perspective publication-title: Curr. Protein Pept. Sci. doi: 10.2174/138920312799277901 – volume: 27 start-page: 7924 year: 1998 ident: 10.1016/j.bbagen.2017.10.015_bb0525 article-title: Interparticle interactions and structural changes of nucleosome Core particles in low-salt solution publication-title: Biochemistry doi: 10.1021/bi00420a051 – volume: 37 start-page: 12443 year: 1998 ident: 10.1016/j.bbagen.2017.10.015_bb0390 article-title: Protein denaturation: a small-angle X-ray scattering study of the ensemble of unfolded states of cytochrome c publication-title: Biochemist doi: 10.1021/bi980535t – volume: 71 start-page: 1051 year: 2015 ident: 10.1016/j.bbagen.2017.10.015_bb0140 article-title: Ambiguity assessment of small-angle scattering curves from monodisperse systems publication-title: Acta Crystallogr. Sect. D: Biol. Crystallogr. doi: 10.1107/S1399004715002576 – volume: 104 start-page: 873 year: 2013 ident: 10.1016/j.bbagen.2017.10.015_bb0410 article-title: Wide-angle X-ray solution scattering for protein-ligand binding: multivariate curve resolution with Bayesian confidence intervals publication-title: Biophys. J. doi: 10.1016/j.bpj.2012.12.019 – volume: 49 start-page: 13 year: 1986 ident: 10.1016/j.bbagen.2017.10.015_bb0560 article-title: Quaternary organization of the 30 S ribosomal subunit of Escherichia coli publication-title: Biophys. J. doi: 10.1016/S0006-3495(86)83573-1 – volume: 11 start-page: 314 year: 2004 ident: 10.1016/j.bbagen.2017.10.015_bb0035 article-title: Liquid-chromatography-coupled SAXS for accurate sizing of aggregating proteins publication-title: J. Synchrotron Radiat. doi: 10.1107/S0909049504014086 – volume: 18 start-page: 5707 year: 2016 ident: 10.1016/j.bbagen.2017.10.015_bb0250 article-title: Deciphering conformational transitions of proteins by small angle X-ray scattering and normal mode analysis publication-title: Phys. Chem. Chem. Phys. doi: 10.1039/C5CP04540A |
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