The use of X-ray lasers to obtain structures and molecular movies in biology is reviewed. Methods include single-particle imaging, serial crystallography and fast solution scattering at room temperature.

Atomistic simulations enhance protein crystallography, yielding mechanistic insights into a protein kinase involved in the regulation of fundamental biological processes that include metabolism, development, memory and immune response.

The enantiotropic relationship between the four polymorphs of pyrazinamide is analyzed by means of accurate X-ray diffraction measurements, normal-mode refinement and periodic DFT calculations.

Polymorphic structural changes in tridymite have been investigated by molecular dynamics simulation. The main polymorphic transitions were reproduced and their mechanisms are explained.

Time-resolved cryo-EM is an emerging technique in structural biology that allows the user to capture structural states which would otherwise be too transient for standard methods. There has been a resurgence in technical advancements in this field in the last five years and this review provides a summary of the technical highlights.

A computational method for obtaining the time-dependent intermediate scattering function of supported membrane stacks is presented.

An X-ray absorption spectroscopy electrochemical cell was used to collect high-quality X-ray absorption spectroscopy measurements of N-truncated Cu:amyloid-β (Cu:Aβ) samples under near-physiological conditions. The geometry of binding sites for the copper binding in Aβ_4–8/12/16 and the ability of these peptides to perform redox cycles in a manner that might produce toxicity in human brains were determined.

This paper presents results of molecular dynamics simulations of gold nanoparticles and their experimental verification by means of X-ray diffraction. The conducted studies reveal that structural disorder in gold nanoclusters is related to surface effects and vacancies.

The catalytic and substrate-regulatory mechanisms of a novel bacterial prolyl oligopeptidase from M. arenaceous (MaPOP) are reported. The suggested substrate-assisted catalytic mechanism of MaPOP may be helpful in understanding the catalytic behavior of prolyl oligopeptidases under physiological conditions.

Ensemble refinement of six protein–ligand crystal structures indicates a much larger flexibility of some amino-acid side chains and ligand groups than is suggested by standard crystallographic refinement. Molecular-dynamics simulations and automatic generation of alternative conformations confirm the high flexibility of these groups, indicating that ensemble refinement can be used to identify such flexible groups.