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Journal Article

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

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Hunte,  Carola
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kao,  Wei-Chun
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Boesecke, P., Bois, J. M., Crépin, T., Hunte, C., Kahn, R., Kao, W.-C., et al. (2009). A first low-resolution difference Fourier map of phosphorus in a membrane protein from near-edge anomalous diffraction. Journal of Synchrotron Radiation, 16(5), 658-665. doi:10.1107/S0909049509025692.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D7C0-6
Abstract
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-50-(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