Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography

Refilling the proton pump Proteins are dynamic. Rearrangements of side chains, secondary structure, and entire domains gate functional transitions on time scales ranging from picoseconds to milliseconds. Weinert et al. used time-resolved serial crystallography to study large conformational changes in the proton pump bacteriorhodopsin that allow for redistribution of protons during the pumping cycle. They adapted methods used for x-ray free electron lasers to synchrotron x-ray sources. Large loop movements and a chain of water molecules were central to regenerating the starting state of bacteriorhodopsin. Science , this issue p. 61