The power of three

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Production, crystallization and X-ray diffraction analysis of the protease CT441 from Chlamydia trachomatis

The C. trachomatis protease CT441 has been recombinantly produced and crystallized, and a diffraction data set has been collected to a resolution of 2.95 Å.

Heterogeneous nucleation is required for crystallization of the ZnuA domain of pneumococcal AdcA

Diffraction-quality crystals of the ZnuA domain of pneumococcal AdcA were obtained using dried seaweed powder as a heterogeneous nucleating agent. X-ray diffraction data were collected to 2.03 Å resolution.

Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada

The restoration of the native form of laccase from B. aclada from the type 2 copper-depleted form of the enzyme was investigated. Copper ions were found to be incorporated into the active site after soaking the depleted enzyme in a Cu⁺-containing solution.

Expression, purification and crystallization of a plant polyketide cyclase from Cannabis sativa

Olivetolic acid cyclase from C. sativa L. has been overexpressed in E. coli, purified and crystallized. Diffraction data have been collected to a resolution of 1.40 Å.

Crystallization behaviour of glyceraldehyde de­hydrogenase from Thermoplasma acidophilum

Wild-type and an F34M+S405N variant of glyceraldehyde dehydrogenase from T. acidophilum were crystallized and X-ray diffraction data were collected for both enzyme variants to resolutions of 1.95 and 2.10 Å, respectively.

Combining dehydration, construct optimization and improved data collection to solve the crystal structure of a CRM1–RanGTP–SPN1–Nup214 quaternary nuclear export complex

The crystal structure determination of a CRM1–RanGTP–SPN1–Nup214 quaternary nuclear export complex is reported. The process included protein-construct optimization, seeding, PEG-mediated crystal dehydration and additional post-mounting steps using an HC1c crystal humidifier.

Structure of Spo0M, a sporulation-control protein from Bacillus subtilis

The crystal structure of Spo0M was determined and the structure of the N-terminal half of Spo0M was compared with other proteins belonging to the arrestin clan. The FP domain of PI31 was also identified as a potential homologue of the C-terminal half of the Spo0M protein.

Seeding for sirtuins: microseed matrix seeding to obtain crystals of human Sirt3 and Sirt2 suitable for soaking

In the present study, microseed matrix seeding was successfully applied to obtain a large number of crystals of the human sirtuin isotypes Sirt2 and Sirt3. These crystals appeared predictably in diverse crystallization conditions, diffracted to a higher resolution than reported in the literature and were subsequently used to study the protein–ligand interactions of two indole inhibitors.

Crystallographic analysis of a cupin superfamily enzyme from Microcystis aeruginosa involved in aeruginosin biosynthesis

The recombinant expression, purification, crystallization and X-ray crystallographic analysis of AerE from M. aeruginosa, an enzyme belonging to the cupin superfamily which has been deduced to participate in the biosynthesis of the 2-carboxy-6-hydroxyoctahydroindole moiety of aeruginosin, are described.

Expression, purification, crystallization and X-ray diffraction analysis of ChiL, a chitinase from Chitiniphilus shinanonensis

The catalytic domain of ChiL, a chitinase from the chitin-degrading bacterium C. shinanonensis, was expressed, purified and crystallized. Preliminary X-ray analysis shows that the crystal belonged to the orthorhombic space group P2₁2₁2₁ and diffracted to 1.25 Å resolution.

Crystallographic insights into the structure–activity relationships of di­azaborine enoyl-ACP reductase inhibitors

Crystallographic studies show that diazaborines lacking a sulfonyl group can successfully inhibit E. coli enoyl-ACP reductase.

Structures of plasmepsin II from Plasmodium falciparum in complex with two hydroxyethylamine-based inhibitors

The crystal structures described here demonstrate the conformational flexibility of the active-site cavity of the plasmepsins. The interactions of the different moieties in the P1′ position of the inhibitors have to be taken into account in the design of new potent plasmepsin inhibitors.

Crystallographic analysis of RsmA, a ribosomal RNA small subunit methyltransferase A from Staphylococcus aureus. Corrigendum

A correction is made to the article by Liu et al. [(2015), Acta Cryst. F71, 1063–1066].