Editorial.

The structure factors deposited with PDB entry 3k78 show properties inconsistent with experimentally observed diffraction data, and without uncertainty represent calculated structure factors. The refinement of the 3k78 model against these structure factors leads to an isomorphous structure different from the deposited model with an implausibly small R value (0.019).

A response to the article by Rupp (2012), Acta Cryst. F68, 366–376.

The structure of the third catalytic domain of the human protein disulfide isomerase ERp46 has been determined to 2.0 Å resolution.

The crystal structure of MurA from the marine Gram-negative bacterium Vibrio fischeri in complex with UNAG and the drug fosfomycin has been solved to a resolution of 1.93 Å.

The crystal structures of the C-terminal domain of S. cerevisiae Avo1 and of its human orthologue Sin1 have been determined. The structures show that the C-termini of the two proteins have the PH-domain fold with a putative binding site for phosphoinositides.

The crystal structure of the tetradecanucleotide sequence d(CCCCGGTACCGGGG)₂ as an A-DNA duplex and its interaction with a manganese ion are described.

The 1.87 Å resolution crystal structure of the His269Arg mutant of rat aldose reductase-like protein (AKR1B14) complexed with NADPH is described.

Two structures of factor XIa in complex with small synthetic inhibitors are reported. These are the first structures of factor XIa complexed to small non-basic inhibitors.

The structure of the nonsteroidal anti-inflammatory drug analogue 3-phenoxybenzoic acid bound to aldo–keto reductase 1C3 (AKR1C3) is presented as a lead for the discovery and development of novel agents for inhibiting AKR1C3, an anticancer target.

The crystal structure of E. coli aspartate α-decarboxylase Asn72Ala reveals the structure of the previously unresolved C-terminus.

Structural data for the ternary complex of P. carinii DHFR with NADPH and the potent inhibitor PY1014 reveal conformational changes that help to explain the weaker potency and selectivity of the pyrido[2,3-d]pyrimidine scaffold compared with the homologous pyrimidine series of antifolates.

A PacL homologue from L. monocytogenes has been purified and crystallized. The crystals diffracted to 3.2 Å resolution.

The crystallization of the ligand-binding domain of the methyl-accepting chemotaxis protein chemoreceptor McpS (McpS-LBD) is reported.

Interleukin-23 (IL-23), a member of the IL-12 family, is a heterodimeric cytokine composed of p19 and p40 subunits. Human p19 and p40 subunits were cloned and coexpressed in N-acetylglucosaminyltransferase I-negative 293S cells. The glycosylated human IL-23 was purified and crystallized by the hanging-drop vapour-diffusion method.

The N-terminal Kunitz domain of boophilin, a specific thrombin inhibitor, was crystallized. The orthorhombic crystals had an unusually low solvent content and diffracted to beyond 0.87 Å resolution at a synchrotron source.

Pyridoxal biosynthesis lyase PdxS from P. horikoshii has been overexpressed and crystallized. X-ray diffraction data have been collected to 2.61 Å resolution.

Crystals of the SCAN domain of Zfp206 are tetragonal, belonging to space group I422 with unit-cell parameters a = 67.57, c = 87.54 Å and one molecule in the asymmetric unit, and diffract to 1.85 Å resolution.

The wild type BFPvv has been crystallized for the first time in order to obtain its tertiary structure and to further understand how chromophore formation occurs via a different oxygen-independent mechanism.

Recombinant AciX9_0562 from Acidobacterium sp. MP5ACTX9 containing sequence motifs characteristic of the RmlC-type cupins superfamily and containing Pfam motif PF07883 has been successfully cloned, expressed and purified, and crystallized in a number of conditions from the Morpheus protein crystallization screen.

UDP-galactopyranose mutase from A. fumigatus was crystallized and structure solution is in progress.

A crystal of nurse shark β₂-microglobulin diffracted to 2.3 Å resolution and belonged to space group P3₂21, with unit-cell parameters a = b = 88.230, c = 67.146 Å and two molecules per asymmetric unit. The Matthews coefficient V _M was calculated to be about 3.28 ų Da⁻¹, corresponding to 62.5% solvent content.

The crystallization and preliminary analysis of two crystal forms of survival protein E from X. fastidiosa are reported.

The luminal domain of human endoplasmic reticulum aminopeptidase 2 has been expressed, purified and crystallized. The crystals belonged to the orthorhombic space group P2₁2₁2 and diffracted anisotropically to 3.3 Å resolution in the best direction on an in-house source.

AAC(6′)-Im is an N-acetyltransferase enzyme responsible for aminoglycoside resistance in E. faecium and E. coli isolates. Crystals of the kanamycin complex of this enzyme have been prepared and preliminary X-ray diffraction experiments have been undertaken.

Protein disulfide isomerase (PDI) is known to bind to the thyroid hormone triiodothyronine (T3). Here, the expression, crystallization and preliminary X-ray studies of the b and b′ domains of rat PDI in ligand-free and T3-complexed states are reported.

Crystals of the abscisic acid receptor PYL3 and of the PYL3–pyrabactin complex were obtained and optimized in order to obtain high-quality diffraction data. Diffraction data sets were collected and processed to 2.5 and 1.83 Å resolution, respectively.

An inactive MaoC-like hydratase mutant from P. capsici was obtained and purified, and the purified mutant was cocrystallized in the presence of the substrate crotonyl-CoA.

Diffraction-quality crystals of the turnip yellow mosaic virus proteinase/ubiquitin hydrolase could only be obtained from a protein preparation that was heavily contaminated with E. coli 30S ribosomal S15 protein. Crystal packing reveals the basis of this observation.

OsAREB8 from rice (O. sativa), a member of the AREB/ABF family of bZIP transcription factors, was expressed, purified and crystallized using the sitting-drop vapour-diffusion method. A crystal of OsAREB8 in complex with its cognate DNA diffracted X-rays to 3.65 Å resolution.

Protein crystals were vitrified using high-pressure freezing in their mother liquor at 210 MPa and 77 K without cryoprotectants or oil coating. The method was successfully applied to photosystem II, which is representative of a membrane protein with a large unit cell and weak crystal contacts.