The main protein from the hemolymph of the cattle tick B. microplus has been crystallized using 1,6-hexanediol. The crystals belonged to the triclinic space group P1 and diffracted up to 2.1 Å resolution.

Crystals of the complex between black-eyed pea trypsin and chymotrypsin inhibitor (BTCI) and bovine β-trypsin diffracted to 2.36 Å resolution and belong to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 59.3, b = 61.8, c = 80.0 Å.

In order to gain new insights into the protein structure and its possible interaction with a metal ion or effector ligand, BigR from X. fastidiosa was crystallized in native and selenomethionine (SeMet) labelled forms using the hanging-drop vapour-diffusion method.

Crystals of infestin 4, a factor XIIa Kazal-type inhibitor from T. infestans, diffracted to 1.8 Å resolution and belong to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 25.89, b = 45.64, c = 57.41 Å.

Crystal structures of factor XIIa inhibitor infestin 4 and infestin 1–trypsin complex have been refined at 1.4 and 2.5 Å resolutions, respectively. Mutants of infestin 4 highly specific to factor XIIa were selected by phage display.

S. parahyba chymotrypsin inhibitor in complex with chymotrypsin has been purified and crystallized using the vapour-diffusion method and preliminarily analysis has been performed using X-ray diffraction.

Recombinant Ohr was expressed in E. coli as a His₆-tagged fusion protein, purified by nickel-affinity chromatography and crystallized using PEG 4000 as precipitant after treatment with t-butyl hydroperoxide. Crystals belong to space group P6₅22, with unit-cell parameters a = b = 87.66, c = 160.28 Å, and diffract X-rays to a resolution of 1.8 Å.

Thioredoxin reductase 1 (Trr1) from S. cerevisiae is a component of the thioredoxin system, which is involved in several biological processes, including the reduction of disulfide bonds and response to oxidative stress. The expression, purification, crystallization and preliminary X-ray crystallographic studies of yeast Trr1 are reported.

The gene coding for Q4DV70 has been cloned and the protein overexpressed in Escherichia coli with an N-­terminal His tag. Purification of Q4DV70 was carried out by affinity and size-exclusion chromatography and the His tag was removed by TEV protease digestion. Crystals of Q4DV70 were grown using the sitting-drop vapour-diffusion method.

A ternary complex of the proteinase inhibitor (BTCI) with trypsin and chymotrypsin was crystallized and its crystal structure was solved by molecular replacement.

The first crystallographic study of a member of the YaeQ family of proteins, which are conserved in a small group of Gram-negative bacteria, most of which are animal or plant pathogens, is reported. Diffraction data were collected to 1.9 Å resolution and an interpretable electron-density map was obtained.

Cloning, expression, purification, crystallization and data collection are reported for a member of the SufE family of proteins involved in the biosynthesis of Fe–S clusters in prokaryotes. Diffraction data were collected to 1.9 Å resolution and an interpretable electron-density map has been obtained by molecular replacement.

The structure of four benzo[b]chalcogenophenes are described. The presence of a phenyl­selanyl group at a vicinal position of bromide or iodine triggers a stabilizing intra­molecular orbital inter­action between a lone pair of electrons of a halogen atom and the anti­bonding σ*_(Se–C) orbital (n_halogen–σ*_(Se–C), resulting in the almost linear alignment of the halogen–selenium–carbon atoms that changes the conformation and also the three-dimensional packing.

The digestive lysozymes 1 and 2 from M. domestica were crystallized by vapour diffusion. The crystallographic data were processed to a maximum resolution of 1.9 Å in both cases.

The structure of E. coli L-asparaginase has been determined at 1.95 Å resolution in space group C2. The crystal structure is compared with the previously determined P2₁ crystal form.

The molybdate-binding protein (ModA) from X. axonopodis pv. citri was crystallized with sodium molybdate in the presence of PEG or sulfate. The crystal diffracted to a maximum resolution of 1.7 Å and belongs to the orthorhombic space group C222_1, with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 Å.

The Xanthomonas axonopodis pv. citri maltose-binding protein MalE has been crystallized at 293 K using the hanging-drop vapour-diffusion method.