Crystal structures of proteins and nucleic acids with data resolution up to 2.2 Å are solved via a novel direct-methods program using the Pattterson map as prior information.

We used on-line in crystallo UV–Vis absorption spectroscopy in conjunction with X-ray crystallography on beamline BM07-FIP2 at the ESRF to compare the structural effects of specific radiation damage on two different metal-containing proteins at either room or cryogenic temperature.

The authors have developed cryoJAX, a cryo-EM image-simulation library for developing data-analysis techniques across cryo-EM modalities. CryoJAX is built on JAX, an emerging scientific computing framework in Python well suited for cryo-EM data analysis.

The Small-Angle Scattering Biological Data Bank (SASBDB) has surpassed 5000 deposited data sets, highlighting its role as a central open-access resource for biological small-angle scattering data and its growing impact on method development, benchmarking and data-driven analysis.

Structural characterization of S. mansoni cathepsin D1 in complex with a nanobody reveals the conformation of the propeptide-bound state and identifies a schistosome-specific epitope.

This work identifies two cysteine residues crucial for the intrinsic stability of the complex between NADPH-dependent thioredoxin reductase C (NTRC) and 2-Cys peroxiredoxin (2CP) and the intermolecular interaction between them, determines the structure of the NTR domain of N. benthamiana NTRC and provides novel mechanistic insights into the NTRC–2CP regulatory complex.

An explicit numerical leveling of non-uniformly distributed sets of 2D projections with the program VUE improves the 3D reconstructions and illustrates sources of image distortion.

We propose a numerical measure to quantify the deviation of a distribution of cryo-EM 2D views from the uniform distribution. This approach allows the traditional two-dimensional projection diagrams to be complemented with quantitative characteristics and simple, easily generated curves that are straightforward to analyze.

It is postulated that the PDB should use the CAVEAT record more prominently to warn scientists using its archives of potential risks and errors.

The construction of a new experimental station for macromolecular crystallography at NanoTerasu under the AMED/BINDS project is presented.

This work demonstrates that multi-position data acquisition mitigates radiation damage in electron diffraction of three-dimensional protein crystals and that merging data from selected crystals in distinct orientations enhances completeness. Application of the two approaches enables high-quality structural models to be obtained from limited or sensitive samples.

YouTube video by International Union of Crystallography

Regulation of pharmaceutical lead compounds does not yet involve the need for patient-relevant macromolecular structures determined at 37°C; nevertheless, we highlight the advantages of these to ensure chemical relevance and the identification of changes which may occur under physiological conditions. The PDB and CSD entries for diffraction data measured at ≥37°C, as well as a cryoEM 37°C freeze-trapped structure, are considered and the description includes structures obtained well above 37°C that are relevant to thermophile and hyperthermophile structural biology.