A high-resolution structure of ligand-free human glutamate carboxypeptidase II

A crystal structure of ligand-free human glutamate carboxypeptidase II refined to 1.65 Å resolution is reported. The structure provides insight into the active-site of the enzyme in its unliganded state.

Structure of the T109S mutant of Escherichia coli di­hydroorotase complexed with the inhibitor 5-fluoroorotate: catalytic activity is reflected by the crystal form

A single-point mutant (T109S) of E. coli dihydroorotase initially crystallizes so that the two monomers of the dimer are related by a crystallographic twofold axis. In the presence of substrate, conversion to the previously observed asymmetric dimer with substrate bound in one subunit and product in the other is observed.

Monellin (MNEI) at 1.15 Å resolution

The crystal structure of the sweet protein MNEI at 1.15 Å resolution reveals networks of alternate conformations and stably bound negative ions.

Structure of 5-formyltetra­hydrofolate cyclo-ligase from Bacillus anthracis (BA4489)

The structure of 5-formyltetrahydrofolate cyclo-ligase from B. anthracis determined by X-ray crystallography at a resolution of 1.6 Å is described.

Structure of a UPF0150-family protein from Thermus thermophilus HB8

The crystal structure of the hypothetical protein TTHA0281 from T. thermophilus HB8 has been determined at 1.9 Å resolution. The TTHA0281 protein forms a homotetramer in which each monomer adopts an α-β-β-β-α fold.

The structure of Plasmodium vivax phosphatidylethanolamine-binding protein suggests a functional motif containing a left-handed helix

The crystal structure of a phosphatidylethanolamine-binding protein from P. vivax, a homolog of Raf-kinase inhibitor protein (RKIP), has been solved to a resolution of 1.3 Å. The inferred interaction surface near the anion-binding site is found to include a distinctive left-handed α-helix.

Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of initiation factor 1 from Mycobacterium tuberculosis

Initiation factor 1 from M. tuberculosis was cloned, expressed, purified and crystallized. A complete data set has been collected to 1.47 Å resolution.

Extracellular overproduction and preliminary crystallographic analysis of a family I.3 lipase

A family I.3 lipase from Pseudomonas sp. MIS38 was secreted from Escherichia coli cells to the external medium, purified and crystallized and preliminary crystallographic studies were performed.

Purification, crystallization and preliminary X-ray diffraction analysis of the non-ATPase subunit Nas6 in complex with the ATPase subunit Rpt3 of the 26S proteasome from Saccharomyces cerevisiae

The complex of the non-ATPase subunit Nas6 with the C-terminal domain of the ATPase subunit Rpt3 of the 26S proteasome from S. cerevisiae was co-expressed in E. coli and purified to homogeneity. The crystals obtained from the protein complex diffracted to a resolution of 2.2 Å.

Purification and crystallization of Kokobera virus helicase

Kokobera virus is a mosquito-borne flavivirus belonging, like West Nile virus, to the Japanese encephalitis virus serocomplex. Crystals of the Kokobera virus helicase domain were obtained by the hanging-drop vapour-diffusion method and exhibit a diffraction limit of 2.3 Å.

Preparation and preliminary X-ray diffraction analysis of crystals of bacterial flagellar sigma factor σ²⁸ in complex with the σ²⁸-binding region of its antisigma factor, FlgM

A complex of E. coli flagellar and chemotaxis-specific sigma factor σ²⁸ bound to the σ²⁸-binding region of its antisigma factor FlgM was crystallized. Diffraction data were collected to a resolution of 2.7 Å.

Crystallization of Saccharomyces cerevisiae aminopeptidase 1, the major cargo protein of the Cvt pathway

Aminopeptidase 1, a cargo protein in the cytosol-to-vacuole targeting (Cvt) pathway, was expressed, purified and crystallized in two crystal forms.

Expression, crystallization and X-ray data collection from microcrystals of the extracellular domain of the human inhibitory receptor expressed on myeloid cells IREM-1

IREM-1 (immune receptor expressed on myeloid cells 1) is an inhibitory receptor of the immunoglobulin superfamily involved in the functional regulation of myeloid cells. It contains an extracellular region comprising one IgV-like domain. The extracellular IgV-like domain, believed to be involved in target-cell recognition, has been expressed in E. coli, folded in vitro and crystallized.

The use of Co²⁺ for crystallization and structure determination, using a conventional mono­chromatic X-ray source, of flax rust avirulence protein

It is demonstrated that anomalous diffraction based on the signal from a cobalt ion measured on a conventional monochromatic X-ray source can be used to determine the structure of a protein with a novel fold (M. lini avirulence protein AvrL567-A). The approach could be applicable to many metal-binding proteins, particularly when synchrotron radiation is not readily available.

Crystallization, diffraction data collection and preliminary crystallographic analysis of hexagonal crystals of Pseudomonas aeruginosa amidase

Crystals of aliphatic amidase (acylamide amidohydrolase; EC 3.5.1.4) from P. aeruginosa were obtained in space group P6₃22 and diffracted to 1.25 Å resolution.

Crystallization and molecular-replacement solution of a diagnostic fluorescent dye in complex with a specific Fab fragment

The complex formed by a Fab antibody fragment and the indotricarbocyanine dye tetrasulfocyanine (TSC) has been crystallized in three different crystal forms. For two of these, data sets were collected, molecular-replacement solutions were identified and refinement has been started.

Crystallization and preliminary X-ray crystallographic study of alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidus

The N- and C-terminal fragments of alanyl-tRNA synthetase from the archaeon A. fulgidus have been crystallized.

Crystallization and preliminary X-ray crystallographic studies of the oligomeric death-domain complex between PIDD and RAIDD

The PIDD DD–RAIDD DD complex has been crystallized. The crystals are hexagonal and belong to space group P6₅, with unit-cell parameters a = b = 138.4, c = 207.6 Å. The crystals were obtained at room temperature; a native crystal diffracted to 3.2 Å resolution and a Hg-derivatized crystal to 4.0 Å resolution.

Crystallization and preliminary X-ray analysis of AbsC, a novel regulator of antibiotic production in Streptomyces coelicolor

A novel regulator of antibiotic production in S. coelicolor, AbsC, has been crystallized in space group P2₁2₁2₁. X-ray data to 2.25 Å resolution were collected on station PX 14.1 at Daresbury.

Crystallization and preliminary X-ray analysis of the O-methyltransferase NovP from the novobiocin-biosynthetic cluster of Streptomyces spheroides

Monoclinic crystals of NovP, an O-methyltransferase from S. spheroides, were obtained and native X-ray data to 1.4 Å resolution were recorded.

Purification, crystallization and preliminary crystallographic analysis of a GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus

A GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus has been crystallized. Combined with biochemical analyses, it is expected that the structure of this protein will give insight in the function of a relatively unknown subfamily of the GTPase superfamily.

Crystallization and preliminary X-ray diffraction studies of trypsin-like proteases from the gastric fluid of the marine crab Cancer pagurus

Two trypsins from the gastric fluid of the marine crab C. pagurus were purified and crystallized and X-ray data were collected to 0.97 and 3.2 Å resolution.

Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis

Enoyl-ACP reductase III (FabL) from B. subtilis has been overexpressed, purified and crystallized. The crystal belongs to space group P622, with unit-cell parameters a = b = 139.56, c = 62.75 Å, α = β = 90, γ = 120°, and data were collected to 2.5 Å resolution using synchrotron radiation.

Crystallization and preliminary X-ray characterization of 1,3-propanediol de­hydrogenase from the human pathogen Klebsiella pneumoniae

1,3-Propanediol dehydrogenase from K. pneumoniae has been overexpressed in E. coli, purified and crystallized. Diffraction data have been collected to 2.7 Å resolution.

Preliminary characterization of (nucleoside-2′-O-)-methyltransferase crystals from Meaban and Yokose flaviviruses. Corrigendum

A corrigendum to the paper by Mastrangelo et al. (2006), Acta Cryst. F62, 768–770.