In this work, serial crystallography is applied to a drug discovery target and the room-temperature ligand-bound complexes are used to explore temperature-dependent structural differences.

Neutron powder diffraction from D-alanine, a D-form amino acid present in higher animals including humans, shows subtle structural differences when compared with its enantiomer, L-alanine. These dissimilarities are due to different rearrangements of the NH₃⁺ group as revealed by Raman scattering.

X-ray crystallography at variable tem­per­ature for SARS-CoV-2 M^pro reveals a com­plex conformational landscape, including a mobile metal at the catalytic dyad, mercurial conformational heterogeneity at various sites, and an intra­molecular network bridging the active site and dimer inter­face.

The uncertainty in temperature-dependent EXAFS measurements on CdTe is discussed, focusing on the first-shell bond thermal expansion, parallel and perpendicular mean square relative displacements and the third cumulant.

The dependences of the crystal structure of CrAs on temperature (30–400 K) and on pressure (0–9.46 GPa) are reported. The investigation shows twinning accompanying the temperature-induced isosymmetrical phase transition and the existence of a distinct Cr–Cr distance within the structure showing anomalous behavior.

A new approach to variable-temperature measurements is presented, where the sample temperature changes continuously as a function of position.

A new temperature-controllable humidifier for X-ray diffraction has been developed. It is shown that the humidifier can successfully maintain protein crystal growth at a temperature lower than room temperature.

Small differences between heavy-atom derivatives can be exploited to improve the experimental phasing by treating each derivative as an independent SAD data set and combining these data sets with circular permutable pairs of SIR data sets. The basis for this generally applicable approach is that the effective resolution of isomorphous signals between highly isomorphous derivatives is often much higher than the effective resolution of the anomalous signals of individual derivative data sets.

It is shown that dimerization is promoted by glycolipid binding to human GLTP. The importance of dimer flexibility in wild-type protein is manifested by point mutation that `locks' the dimer while diversifying ligand/protein adaptations.

Solid-state phenomena like disorder, polymorphism but also the occurrence of high-Z′ crystal structures can be linked via energy differences in `archetype crystal structures', which will permit better prediction of their occurrence.