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 …

Traditionally, crystallographic analysis of macromolecules has depended on large, well-
ordered crystals, which often require significant effort to obtain. Even sizable crystals …

Macromolecular crystallography at synchrotron sources has proven to be the most influential
method within structural biology, producing thousands of structures since its inception. While …

Thanks to recent technological advances in X-ray and micro-electron diffraction and solid-
state NMR, structural information can be obtained by using much smaller crystals. Thus …

Sarcoendoplasmic reticulum calcium ATPase (SERCA), a member of the P-type ATPase
family of ion and lipid pumps, is responsible for the active transport of Ca2+ from the …

Macromolecular crystallography was immensely successful in the last two decades. To a
large degree this success resulted from use of powerful third generation synchrotron x-ray …

High-throughput X-ray crystal structures of protein–ligand complexes are critical to
pharmaceutical drug development. However, cryocooling of crystals and X-ray radiation …

Highlights•Serial femtosecond crystallography studies of membrane proteins.•Damage free
structures of membrane proteins collected using XFEL radiation.•Serial millisecond …

Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) is a novel
tool in structural biology. In contrast to conventional crystallography, SFX relies on merging …