Correlated motions of protein atoms are of biological significance in processes involving ligand binding, conformational change and information transmission. X-ray scattering patterns from protein crystals contain diffuse scattering that originates from correlated displacements of atoms. Here we present experimental data on diffuse X-ray scattering from lysozyme crystals. We show that the diffuse scattering is similar in form to scattering derived from molecular dynamics simulation and normal mode analysis of the isolated protein, the normal modes giving the closest agreement with experiment.
A new multichannel collimator optimized for Paris–Edinburgh press geometry and a two-dimensional imaging plate detector have been developed at beamline ID30 at the European Synchrotron Radiation Facility. This system allows in situ collection of high quality x-ray diffraction data of liquids and amorphous materials simultaneously at high pressure and high temperature conditions. Excellent improvements in terms of signal to background ratio have been obtained. In order to illustrate the potential of this new device, preliminary results on liquid tin and lead under high pressure are presented.
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