High-throughput structures of protein-ligand complexes at room temperature using serial femtosecond crystallography.

ABSTRACT: High-throughput X-ray crystal structures of protein-ligand complexes are critical to pharmaceutical drug development. However, cryocooling of crystals and X-ray radiation damage may distort the observed ligand binding. Serial femtosecond crystallography (SFX) using X-ray free-electron lasers (XFELs) can produce radiation-damage-free room-temperature structures. Ligand-binding studies using SFX have received only modest attention, partly owing to limited beamtime availability and the large quantity of sample that is required per structure determination. Here, a high-throughput approach to determine room-temperature damage-free structures with excellent sample and time efficiency is demonstrated, allowing complexes to be characterized rapidly and without prohibitive sample requirements. This

SUBMITTER: Moreno-Chicano T 

PROVIDER: S-EPMC6830213 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature