A first low-resolution difference Fourier map of phosphorus in a membrane protein from near-edge anomalous diffraction

• Published in: Journal of synchrotron radiation Vol. 16; no. 5; pp. 658 - 665
• Main Authors: Boesecke, Peter, Bois, Jean Marie, Crépin, Thibaut, Hunte, Carola, Kahn, Richard, Kao, Wei-Chun, Nauton, Lionel, Winther, Anne-Marie Lund, Moller, Jesper, Nissen, Poul, Nury, Hughes, Olesen, Claus, Pebay-Peyroula, Eva, Vicat, Jean, Stuhrmann, Heinrich
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.09.2009
• Subjects: anomalous dispersion; Crystallography, X-Ray - methods; Fourier Analysis; membrane proteins; Membrane Proteins - chemistry; nucleoproteins; phosphorus; Phosphorus - analysis
• ISSN: 1600-5775; 0909-0495; 1600-5775
• DOI: 10.1107/S0909049509025692

Crystal diffraction of three membrane proteins (cytochrome bc1 complex, sarcoplasmic reticulum Ca2+ ATPase, ADP‐ATP carrier) and of one nucleoprotein complex (leucyl tRNA synthetase bound to tRNAleu, leuRS:tRNAleu) was tested at wavelengths near the X‐ray K‐absorption edge of phosphorus using a new set‐up for soft X‐ray diffraction at the beamline ID01 of the ESRF. The best result was obtained from crystals of Ca2+ ATPase [adenosin‐5′‐(β,γ‐methylene) triphosphate complex] which diffracted out to 7 Å resolution. Data were recorded at a wavelength at which the real resonant scattering factor of phosphorus reaches the extreme value of −20 electron units. The positions of the four triphosphates of the monoclinic unit cell of the ATPase have been obtained from a difference Fourier synthesis based on a limited set of anomalous diffraction data.