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

The current state-of-the-art experiments in time-resolved structural biology are undoubtedly
the recent extremely impressive results that are emerging from XFEL-based experiments …

X-ray crystallography enables detailed structural studies of proteins to understand and
modulate their function. Conducting crystallographic experiments at cryogenic temperatures …

The high peak brilliance and femtosecond pulse duration of X-ray free-electron lasers
(XFELs) provide new scientific opportunities for experiments in physics, chemistry and …

Highly efficient data-collection methods are required for successful macromolecular
crystallography (MX) experiments at X-ray free-electron lasers (XFELs). XFEL beamtime is …

Radiation damage limits the accuracy of macromolecular structures in X-ray crystallography.
Cryogenic (cryo-) cooling reduces the global radiation damage rate and, therefore, became …

An approach is demonstrated to obtain, in a sample-and time-efficient manner, multiple dose-
resolved crystal structures from room-temperature protein microcrystals using identical fixed …

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 …

X-ray free-electron lasers (XFELs) enable obtaining novel insights in structural biology. The
recently available MHz repetition rate XFELs allow full data sets to be collected in shorter …

Serial crystallography has enabled the study of complex biological questions through the
determination of biomolecular structures at room temperature using low X-ray doses …