Measuring and modeling diffuse scattering in protein X-ray crystallography.

ABSTRACT: X-ray diffraction has the potential to provide rich information about the structural dynamics of macromolecules. To realize this potential, both Bragg scattering, which is currently used to derive macromolecular structures, and diffuse scattering, which reports on correlations in charge density variations, must be measured. Until now, measurement of diffuse scattering from protein crystals has been scarce because of the extra effort of collecting diffuse data. Here, we present 3D measurements of diffuse intensity collected from crystals of the enzymes cyclophilin A and trypsin. The measurements were obtained from the same X-ray diffraction images as the Bragg data, using best practices for standard data collection. To model the underlying dynamics in a practical way that could be used duri

SUBMITTER: Van Benschoten AH 

PROVIDER: S-EPMC4839442 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature