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In a new crystal form of PSAO, the homodimeric molecules lack twofold symmetry and the C-termini of the two protomers are linked by a previously unrevealed disulfide bond.
The amidase from G. pallidus RAPc8, a moderate thermophile, converts amides to the corresponding acids and ammonia and has application as an industrial catalyst. RAPc8 amidase has been cloned, expressed and purified, and then crystallized using the hanging-drop vapour-diffusion method.
The structure of HLA-A*1101 in complex with a HBV peptide homologue is presented and discussed in the context of vaccine design.
The crystal structure of l-lactate oxidase (LOX) from A. viridans at 2.1 Å resolution.
The structure of the second helicase domain of the B. subtilis YxiN protein, a DEAD-box RNA helicase, is presented.
The crystal structure of the 2′-5′ RNA ligase PH0099 from P. horikoshii OT3 was solved at 1.94 Å resolution. The molecule has a bilobal α+β arrangement with two antiparallel β-sheets constituting a V-shaped active-site cleft, as found in other members of the 2H phosphoesterase superfamily.
SIRAS phasing techniques have been employed to determine the structure Mycobacterium tuberculosis Rv1873 at a resolution of 1.38 Å. We show that this conserved hypothetical protein of unknown function shows limited structural similarity to other molecules.
UDP-N-acetylglucosamine pyrophosphorylase was purified and crystallized and X-ray diffraction data were collected to 2.3 Å resolution.
Crystals of 6-aminohexanoate-cyclic-dimer hydrolase were obtained by the sitting-drop vapour-diffusion method using sodium citrate as a precipitant. Diffraction data from native and mercury-derivative crystals were collected to resolutions of 1.90 and 2.06 Å, respectively.
The terminal oxygenase component of carbazole 1,9a-dioxygenase from N. aromaticivorans IC177 was crystallized and diffraction data were collected to 2.30 Å resolution.
The FadA adhesin from F. nucleatum, which is involved in bacterial attachment and invasion of human oral epithelial cells, has been crystallized in space group P61 or P65, and X-ray data have been collected to 1.9 Å resolution.
Expression, crystallization and preliminary X-ray diffraction studies of a novel bifunctional N-acetylglutamate synthase/kinase from X. campestris homologous to vertebrate N-acetylglutamate synthase are reported.
The dihydropyrimidinase from S. meliloti CECT4114, with activity towards both hydantoin and dihydrouracil substrates, was crystallized, and diffraction data were collected to 1.85 Å resolution.
A water-soluble mutant of the outer membrane lipoprotein NlpE has been overexpressed, purified and crystallized. Diffraction data from two crystal forms obtained under two different conditions were collected to 2.8 and 3.0 Å resolution and processed in space groups P43212 and C2, respectively.
Uracil N-glycosylase from M. tuberculosis has been crystallized in complex with a proteinaceous inhibitor (Ugi) and X-ray diffraction data have been collected.
Various truncated and mutant forms of the protease VP4 from infectious pancreatic necrosis virus were used to generate two different crystal forms of VP4 which diffracted to beyond 2.4 Å resolution.
The Kunitz-type trypsin/chymotrypsin inhibitor isolated from C. papaya latex has been crystallized using the hanging-drop vapour-diffusion method. Two different crystal forms are observed, diffracting to 2.6 and 1.7 Å.
Crystallization and preliminary X-ray analysis of a native human tRNA synthetase whose allelic variants are associated with Charcot–Marie–Tooth Disease.
A pseudo death-effector domain (pDED) of HIPPI, a partner of Huntingtin-interacting protein HIP1, has been cloned, overexpressed and crystallized. The crystals of pDED-HIPPI diffracted to 2.2 Å.
A construct of the Cyanothece 51142 pentapeptide-repeat protein Rfr23 (Thr27–Asp174) has been cloned, overexpressed in E. coli and purified. Diffraction data that extend to 2.5 Å and preliminary analyses are reported for selenomethionine-labeled crystals that belong to space group I41.
S. aureus thioredoxin was crystallized using a combination of seeding and site-specific mutagenesis.
The bicupin YwfC from B. subtilis was crystallized in two crystal forms and diffraction data were collected to 2.2 Å resolution.
A HIT-like protein from the plant pathogen X. campestris pathovar campestris has been overexpressed in E. coli, purified and crystallized. The crystals diffract to 1.3 Å.
Preliminary X-ray crystallographic study of a proline-specific aminopepitdase from Aneurinibacillus sp, strain AM-1 was carried out.
Preliminary crystallographic studies on 2-dehydro-3-deoxygalactarate aldolase from L. interrogans.
Crystals of baculovirus-expressed adeno-associated virus serotype 1 (AAV1) capsids have been grown in the rhombohedral space group R32 (unit-cell parameters a = 254.7 Å, α = 62.3°) and shown to diffract X-rays to at least 2.5 Å resolution.
The crystallization and preliminary X-ray analysis of SoxR from E. coli and its complex with DNA are reported.
The N-terminal receptor-binding domain of the FedF adhesin from enterotoxigenic E. coli has been crystallized. This required the deletion of its first 14 residues, which are also cleaved off naturally.
The complexes of human MTH1 with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP, were crystallized. The crystals diffracted to 1.95 and 2.22 Å resolution, respectively.
Perakine reductase, a novel member of the aldo-keto reductase enzyme superfamily of higher plants, is involved in the biosynthesis of monoterpenoid indole alkaloids in the Indian medicinal plant Rauvolfia serpentina. The enzyme has been crystallized in C-centered orthorhombic space group and diffracts to 2.0 Å resolution.
Two thermostable DNA nucleases from archaea were crystallized in different space groups; the crystals were suitable for X-ray analysis.
A study on the crystallization of ornithine acetyltransferase from yeast, catalysing the fifth step in microbial arginine synthesis, is presented. The use of the counter-diffusion technique removes the disorder present in one dimension in crystals grown by either batch or hanging-drop techniques.
Alditol oxidase oxidizes a range of alditols into the corresponding aldoses and is an interesting candidate for biotechnological applications. Crystals of alditol oxidase from S. coelicolor A3(2) were obtained by the hanging-drop vapour-diffusion method and diffracted to 1.1 Å resolution.