The Azotobacter vinelandii FeSII protein forms an oxygen-resistant complex with the nitrogenase MoFe and Fe proteins.

4,4′-{9,9′-Spirobi[10H-acridine]-10,10′-di­yl}di­benzoic acid was designed and synthesized as a new donor–acceptor motif mol­ecule and applied as a ligand with Cd as a metal connector to form a one-dimensional coordination polymer. Both the ligand and the polymer present a sky-blue TADF emission, together with a photoluminescence quantum yield of 40%.

The aliphatic dipeptide alanine–isoleucine (Ala–Ile), protected with a benzyl­oxycarbonyl (Z) group at the N-terminus, forms hollow microtubes with ortho­rhom­bic symmetry upon evaporation on glass surfaces, as shown by field emission scanning electron microscopy (FESEM). These findings provide an increased understanding of the correlation between the single-crystal structure of the peptide building block and its self-assembly mechanism, and expand the library of available building blocks for microtechnological applications.

The High-Pressure Freezing Laboratory for Macromolecular Crystallography (HPMX) at the ESRF allows the preparation of gas derivatives of macromolecular crystals suitable for X-ray diffraction data collection on macromolecular crystallography beamlines. Information obtained from pressurized crystals and/or gas-derivatized structures enables the improved understanding of specific issues in structural biology, such as the internal functional architecture of proteins, the interactions and reactivity of gases with macromolecules and functional structural changes including ligand-binding processes.

The gene encoding a novel bacterial class V dye-decolourizing peroxidase (DyP) from the extremely radiation-resistant and desiccation-resistant bacterium Deinococcus radiodurans was cloned and optimum conditions for high-yield expression were identified. The optimized crystals diffracted to 2.2 Å resolution and the initial characterization and crystallographic analysis is promising with respect to providing highly desired insights into this largely unknown family of DyPs.

inserexs is an open-source program that allows resonant elastic X-ray scattering users to choose the best conditions to determine any parameter of interest (atomic position, occupancy etc.) before an experiment is carried out.

The crystallization of the TLDc domain of oxidation resistance protein 2 from zebrafish is reported.

A system engineered to produce a large-scale structural change from X-ray-induced di­sulfide bond cleavage allows residue-specific changes to be interpreted with SAXS. This system is used to investigate how radical scavengers reduce bond breakage during data collection at 10°C with the results providing insight into mitigation strategies for crystallographic and solution experiments.

In the mol­ecular structure of the title compound, the urethane function and the benzoyl group are almost perpendicular to each other [dihedral angle 88.97 (5)°]. In the crystal structure, infinite supra­molecular layers in the bc plane are formed by weak C—HO hydrogen bonds.

The crystal structure of mycothiol disulfide reductase (Mtr) was determined for the first time. The structure shows a highly conserved and enlarged substrate-binding pocket, providing insight into the substrate-binding mode and specificity of Mtrs.