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

A new scientific frontier opened in 2009 with the start of operations of the world's first x-ray
free-electron laser (FEL), the Linac Coherent Light Source (LCLS), at SLAC National …

Photosystem II (PSII) catalyses the oxidation of water through a four-step cycle of S i states
(i= 0–4) at the Mn4CaO5 cluster,–, during which an extra oxygen (O6) is incorporated at the …

Photosystem II (PSII) is a huge membrane-protein complex consisting of 20 different
subunits with a total molecular mass of 350 kDa for a monomer. It catalyses light-driven …

Historically, room-temperature structure determination was succeeded by cryo-
crystallography to mitigate radiation damage. Here, we demonstrate that serial millisecond …

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 …

Protein crystallography using synchrotron radiation sources has had a tremendous impact
on biology, having yielded the structures of thousands of proteins and given detailed insight …

X-ray crystallography at X-ray free-electron laser sources is a powerful method for studying
macromolecules at biologically relevant temperatures. Moreover, when combined with …

The development and application of the free-electron X-ray laser (XFEL) to structure and
dynamics in biology since its inception in 2009 are reviewed. The research opportunities …

This review is focused on free-electron lasers (FELs) in the hard to soft x-ray regime. The
aim is to provide newcomers to the area with insights into: the basic physics of FELs, the …