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

In this review, we describe recent research developments into radiation damage effects in
macromolecular X-ray crystallography observed at synchrotrons and X-ray free electron …

Cryogenic electron microscopy (cryo-EM) maps are now at the point where resolvability of
individual atoms can be achieved. However, resolvability is not necessarily uniform …

The new European X-ray Free-Electron Laser is the first X-ray free-electron laser capable of
delivering X-ray pulses with a megahertz inter-pulse spacing, more than four orders of …

X-ray-based analytics are routinely applied in many fields, including physics, chemistry,
materials science, and engineering. The full potential of such techniques in the life sciences …

X-ray free-electron lasers have opened up the possibility of structure determination of
protein crystals at room temperature, free of radiation damage. The femtosecond-duration …

Radiation damage inflicted during diffraction data collection in macromolecular
crystallography has re-emerged in the last decade as a major experimental and …

X-ray free-electron lasers have enabled new approaches to the structural determination of
protein crystals that are too small or radiation-sensitive for conventional analysis. For …

Micro-crystal electron diffraction (MicroED) combines the efficiency of electron scattering
with diffraction to allow structure determination from nano-sized crystalline samples in …

A new approach for collecting data from many hundreds of thousands of microcrystals using
X-ray pulses from a free-electron laser has recently been developed. Referred to as serial …