David Arnlund

TL;DR: Serial femtosecond crystallography (SFX) is applied using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals of the well-characterized model protein lysozyme, demonstrating the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

TL;DR: The structure reveals the mechanism of native TbCatB inhibition and demonstrates that new biomolecular information can be obtained by the “diffraction-before-destruction” approach of x-ray free-electron lasers from hundreds of thousands of individual microcrystals.

TL;DR: Measurements indicate that current X-ray free-electron laser technology should enable structural determination from submicrometre protein crystals with atomic resolution, and the shortest apparent pulse lengths occur at the highest resolution.

TL;DR: The first time-resolved femtosecond serial X-ray crystallography results from an irreversible photo-chemical reaction at the Linac Coherent Light Source are obtained.

TL;DR: This work demonstrates an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein, providing direct structural evidence for a 'protein quake'.