With the advent of X-ray free-electron lasers (XFELs), new, high-throughput serial
crystallography techniques for macromolecular structure determination have emerged …

BACKGROUND Conformational changes are essential for the correct functioning of
biological macromolecules. Time-resolved x-ray crystallography extends an extremely …

INTRODUCTION Retinal is a light-sensitive protein ligand that is used by all domains of life
to process the information and energy content of light. Retinal-binding proteins are integral …

The photoisomerization reaction of a fluorescent protein chromophore occurs on the ultrafast
timescale. The structural dynamics that result from femtosecond optical excitation have …

Chloride transport by microbial rhodopsins is an essential process for which molecular
details such as the mechanisms that convert light energy to drive ion pumping and ensure …

Chromophore cis/trans photoisomerization is a fundamental process in chemistry and in the
activation of many photosensitive proteins. A major task is understanding the effect of the …

Hybrid methods that combine quantum mechanics (QM) and molecular mechanics (MM) can
be applied to studies of reaction mechanisms in locations ranging from active sites of small …

Highlights•Time-resolved serial femtosecond crystallography (tr-SFX) probes structure and
function in each sample.•X-ray free electron lasers (XFELS) provide atomic and electronic …

Photolyases, a ubiquitous class of flavoproteins, use blue light to repair DNA photolesions.
In this work, we determined the structural mechanism of the photolyase-catalyzed repair of a …

Bacteriorhodopsin (bR) is a light-driven proton pump. The primary photochemical event
upon light absorption is isomerization of the retinal chromophore. Here we used time …