S. Mous

TL;DR: In this article, the structural changes in the light-driven proton-pump bacteriorhodopsin over 200 milliseconds in time were recorded using synchrotrons.

TL;DR: Crystallographic ‘snapshots’ taken at intervals of femtoseconds to milliseconds after activation show how a light-activated sodium pump carries sodium ions across the cell membrane and provide direct molecular insight into the dynamics of active cation transport across biological membranes.

TL;DR: This work adapted time-resolved serial crystallography developed at X-ray lasers to visualize protein motions using synchrotrons and recorded the structural changes upon proton pumping in bacteriorhodopsin over 200 ms in time.

TL;DR: A molecular movie reveals how ion transport is initiated and controlled in a chloride-pumping rhodopsin, and proposes key mechanistic features enabling finely controlled chloride transport across the cell membrane in this light-powered chloride ion pump.

TL;DR: In this paper , the authors used ultrafast time-resolved crystallography at room temperature to determine how an isomerized twisted all-trans retinal stores the photon energy that is required to initiate the protein conformational changes associated with the formation of the G protein-binding signalling state.