%0 journal article
%@ 0909-0495
%A Boesecke, P.,Bois, J.M.,Crepin, T.,Hunte, C.,Kahn, R.,Kao, W.-C.,Nauton, L.,Winther, A.-M.L.,Moller, J.,Nissen, P.,Nury, H.,Olesen, C.,Pebay-Peyroula, E.,Vicat, J.,Stuhrmann, H.B.

%D 2009
%J Journal of Synchrotron Radiation
%N 5
%P 658-665 
%R doi:10.1107/S0909049509025692
%T A first low-resolution difference Fourier map of phosphorus in a membrane protein from near-edge anomalous diffraction
%U https://doi.org/10.1107/S0909049509025692
5 
%X 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'-([beta],[gamma]-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.