Solving protein structure from sparse serial microcrystal diffraction data at a storage-ring synchrotron source.

ABSTRACT: In recent years, the success of serial femtosecond crystallography and the paucity of beamtime at X-ray free-electron lasers have motivated the development of serial microcrystallography experiments at storage-ring synchrotron sources. However, especially at storage-ring sources, if a crystal is too small it will have suffered significant radiation damage before diffracting a sufficient number of X-rays into Bragg peaks for peak-indexing software to determine the crystal orientation. As a consequence, the data frames of small crystals often cannot be indexed and are discarded. Introduced here is a method based on the expand-maximize-compress (EMC) algorithm to solve protein structures, specifically from data frames for which indexing methods fail because too few X-rays are diffracted into

SUBMITTER: Lan TY 

PROVIDER: S-EPMC6126656 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature