SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique.

ABSTRACT: A significant problem in biological X-ray crystallography is the radiation chemistry caused by the incident X-ray beam. This produces both global and site-specific damage. Site specific damage can misdirect the biological interpretation of the structural models produced. Cryo-cooling crystals has been successful in mitigating damage but not eliminating it altogether; however, cryo-cooling can be difficult in some cases and has also been shown to limit functionally relevant protein conformations. The doses used for X-ray crystallography are typically in the kilo-gray to mega-gray range. While disulfide bonds are among the most significantly affected species in proteins in the crystalline state at both cryogenic and higher temperatures, there is limited information on their response to low X

SUBMITTER: Stachowski TR 

PROVIDER: S-EPMC7671560 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature