Crystal contact-free conformation of an intrinsically flexible loop in protein crystal: Tim21 as the case study

• Published in: Biochimica et biophysica acta. General subjects Vol. 1864; no. 2; p. 129418
• Main Authors: Bala, Siqin, Shinya, Shoko, Srivastava, Arpita, Ishikawa, Marie, Shimada, Atsushi, Kobayashi, Naohiro, Kojima, Chojiro, Tama, Florence, Miyashita, Osamu, Kohda, Daisuke
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.02.2020
• Subjects: case studies; Crystal contact-free space; crystallography; crystals; Flexible loop; Fusion protein; multidimensional scaling; NMR structure; nuclear magnetic resonance spectroscopy; proteins; Solution conformation; Yeast Tim21; yeasts; NMR structure; Yeast Tim21; Solution conformation; Tim21; 2019_NMR; Crystal contact-free space; RDC; CCFS; 2006_crystal; MD; Flexible loop; 2014_NMR; rms; MBP; Fusion protein; MDS

In protein crystals, flexible loops are frequently deformed by crystal contacts, whereas in solution, the large motions result in the poor convergence of such flexible loops in NMR structure determinations. We need an experimental technique to characterize the structural and dynamic properties of in...