Ab initio phasing of the diffraction of crystals with translational disorder.

ABSTRACT: To date X-ray protein crystallography is the most successful technique available for the determination of high-resolution 3D structures of biological molecules and their complexes. In X-ray protein crystallography the structure of a protein is refined against the set of observed Bragg reflections from a protein crystal. The resolution of the refined protein structure is limited by the highest angle at which Bragg reflections can be observed. In addition, the Bragg reflections alone are typically insufficient (by a factor of two) to determine the structure ab initio, and so prior information is required. Crystals formed from an imperfect packing of the protein molecules may also exhibit continuous diffraction between and beyond these Bragg reflections. When this is due to random displacemen

SUBMITTER: Morgan AJ 

PROVIDER: S-EPMC6302929 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature