Karol Nass

TL;DR: Time-resolved serial femtosecond crystallography at an x-ray free-electron laser is used to resolve the ultrafast structural changes in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond and supports the prediction that an immediate collective response of the protein occurs upon ligand dissociation.

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 SwissFEL X-ray Free Electron Laser (XFEL) facility as discussed by the authors started construction at the Paul Scherrer Institute (Villigen, Switzerland) in 2013 and will be ready to accept its first users in 2018 on the Aramis hard Xray branch.

TL;DR: The principal mechanism of isomerization in this prototypical retinal-binding protein has direct relevance for all other members of this important family of membrane proteins, and it provides insight into how protein environments catalyze photochemical reactions in general.

TL;DR: X-ray FEL data can be used for de novo protein structure determination, that is, without previous knowledge about the structure, and high-quality diffraction intensities are obtained, resulting in an experimental electron density map good enough for automated building of the protein structure.