Fixed target combined with spectral mapping: approaching 100% hit rates for serial crystallography.

ABSTRACT: The advent of ultrafast highly brilliant coherent X-ray free-electron laser sources has driven the development of novel structure-determination approaches for proteins, and promises visualization of protein dynamics on sub-picosecond timescales with full atomic resolution. Significant efforts are being applied to the development of sample-delivery systems that allow these unique sources to be most efficiently exploited for high-throughput serial femtosecond crystallography. Here, the next iteration of a fixed-target crystallography chip designed for rapid and reliable delivery of up to 11 259 protein crystals with high spatial precision is presented. An experimental scheme for predetermining the positions of crystals in the chip by means of in situ spectroscopy using a fiducial system for

SUBMITTER: Oghbaey S 

PROVIDER: S-EPMC5937680 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature