| 19713640 |
Boesecke P, Bois JM, Crepin T, Hunte C, Kahn R, Kao WC, Nauton L, Winther AM, Moller J, Nissen P, Nury H, Olesen C, Pebay-Peyroula E, Vicat J, Stuhrmann H: A first low-resolution difference Fourier map of phosphorus in a membrane protein from near-edge anomalous diffraction. J Synchrotron Radiat. 2009 Sep;16(Pt 5):658-65. Epub 2009 Jul 8.
Crystal diffraction of three membrane proteins (cytochrome bc (1) complex, sarcoplasmic reticulum Ca (2+) 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 Ca (2+) ATPase [adenosin-5'-(beta,gamma-methylene) triphosphate complex] which diffracted out to 7 A 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. |
33(0,1,1,3) |