Room-temperature serial synchrotron crystallography of Drosophila cryptochrome.

ABSTRACT: Fixed-target serial crystallography allows the high-throughput collection of diffraction data from small crystals at room temperature. This methodology is particularly useful for difficult samples that have sensitivity to radiation damage or intolerance to cryoprotection measures; fixed-target methods also have the added benefit of low sample consumption. Here, this method is applied to the structure determination of the circadian photoreceptor cryptochrome (CRY), previous structures of which have been determined at cryogenic temperature. In determining the structure, several data-filtering strategies were tested for combining observations from the hundreds of crystals that contributed to the final data set. Removing data sets based on the average correlation coefficient among equivalent r

SUBMITTER: Schneps CM 

PROVIDER: S-EPMC9344480 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature