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Three structures of a putative RNA 5-methyluridine methyltransferase from T. thermophilus, including its complex with S-adenosyl-l-homocysteine, are presented. The structures reveal the mode of cofactor binding, architecture of the putative active site, and the presence of a deep cleft adjacent to the active site that may bind RNA.
The Trypanosoma cruzi dihydroorotate dehydrogenase, a key enzyme in pyrimidine de novo biosynthesis and redox homeostasis, was crystallized in complex with its first reaction product, orotate.
Recombinant squid calexcitin has been crystallized using the hanging-drop vapour-diffusion technique in the orthorhombic space group P212121.
A new myotoxic Lys49-phospholipase from B. moojeni has been crystallized and X-ray diffraction data were collected to 2.18 Å resolution. Preliminary analysis indicates the presence of four molecules in the asymmetric unit, leading to a possible new oligomeric structure for Lys49-PLA2s.
An 8 kDa proteolytic fragment of the A. majus RADIALIS protein was crystallized and X-ray data were collected to 2 Å resolution.
Human agmatinase (Ala36–Val352) was overexpressed and crystallized, and X-ray diffraction data were collected to 2.49 Å.
The putative GTPase PH0525 from P. horikoshii OT3 was crystallized using the microbatch method. Crystals were formed under two different conditions, providing two distinct crystal forms. Diffraction data from the two forms were measured to resolution limits of 2.30 and 2.40 Å and processed in space groups P21 and C2221, respectively.
This article describes the high-level expression, purification and crystallization as well as preliminary X-ray diffraction study of a family 18 chitinase, chitinase A from V. carchariae.
The wild-type editing CP1 domain of A. aeolicus leucyl-tRNA synthetase and two mutant CP1 domains have been overexpressed, purified and crystallized. X-ray diffraction data have been collected to 1.8 Å, which has enabled determination of the structures by molecular replacement.
A DEDDh-type 3′-5′ oligoribonuclease from the plant pathogen X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. The crystals diffracted to 2.1 Å with good quality.
The thioredoxin reductase isolated from S. solfataricus has been crystallized. Diffraction data have been collected from the wild type and from the NADP-bound form of the enzyme to 1.80 and 1.95 Å, respectively. The structure of the thioredoxin reductase has been solved using MAD diffraction data.
Crystallization and preliminary X-ray diffraction studies are reported for a novel Kunitz-type protease inhibitor from B. bauhinioides which contains no disulfide bridges.
A P. furiosus stand-alone RAM domain with hydrolytic activity has been cloned and expressed in E. coli. The purified protein was crystallized alone and with EPNP and PMSF, producing crystals that yield diffraction data to resolutions of 2.8, 2.2 and 2.8 Å, respectively.
The production, purification, crystallization and preliminary crystallographic analysis of empty adeno-associated virus serotype 5 capsids are reported.
The coral-derived cyan fluorescent protein dsFP483 has been crystallized and diffraction data were collected to 2.1 Å. A molecular-replacement solution is presented for 83% of the protein contents of the asymmetric unit.
The Walker-type ATPase PABY2304 of P. abyssi has been cloned, overexpressed, purified and crystallized. X-ray diffraction data from selenomethionine-derivative crystals have been collected to 2.6 Å. The structure has been solved by MAD techniques.
Single crystals of 6-aminohexanoate-dimer hydrolase have been prepared by the sitting-drop vapour-diffusion method using ammonium sulfate as a precipitant. Diffraction data were collected from native and methylmercuric chloride derivative crystals to resolutions of 1.75 and 1.80 Å, respectively.
The lectin from the Nigerian legume B. mildbraedii was crystallized in complex with Man(α1-2)Man and data were collected to a resolution of 1.90 Å using synchrotron radiation.
Recombinant cryptochrome 3 from A. thaliana with FAD and MTHF cofactors has been crystallized using the hanging-drop vapour-diffusion technique in the orthorhombic space group P212121 and X-ray diffraction data were collected to 1.9 Å resolution.
Crystallization of HLA-B*2704 in complex with two peptides.
Acylaminoacyl peptidase from porcine liver has been crystallized. Data were collected to 3.4 Å from native crystals and a search for heavy-atom derivatives is in progress.
Structural informatics and modelling correctly predicted that substrate was required to obtain diffracting crystals of the first characterized nitrile oxidoreductase: the homododecameric QueF.
The CcdA C-terminal domain was crystallized in complex with CcdB in two crystal forms that diffract to beyond 2.0 Å resolution.
Crystallization of the Dickerson dodecamer d(CGCGAATT*CGCG) containing an extra ribose in a phosphodiester linkage is reported.
Crystallization of the human CHP2–NHE1 binding domain complex.