Structures of two superoxide dismutases from Bacillus anthracis reveal a novel active centre

The crystal structures of two manganese superoxide dismutases from B. anthracis were solved by X-ray crystallography using molecular replacement.

A double mutation of Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphate

A double mutation designed to disrupt binding of isoprenoid diphosphate to an enzyme involved in isoprenoid biosynthesis was made and the structure determined. Despite the removal of six hydrogen-bonding interactions, the ligand, acquired during production in E. coli, remains bound. The reasons for this are discussed.

The structure at 1.7 Å resolution of the protein product of the At2g17340 gene from Arabidopsis thaliana

The crystal structure of the 40.8 kDa At2g17340 protein from A. thaliana was determined at 1.7 Å resolution. The structure provides the first insight into the structural organization of the Pfam01937.11 family and establishes that the proteins of this family coordinate a metal in its putative active site.

The first crystal structure of an archaeal helical repeat protein

The crystal structure of ST1625p, a protein encoded by a hypothetical open reading frame ST1625 in the genome of the hyperthermophilic archaeon Sulfolobus tokodaii, was determined at 2.2 Å resolution. The structure of ST1625p consists of a unique superhelix with a low-level structure resemblance to doamins from other proteins with known three-dimensional structures.

Structure of a NAD kinase from Thermotoga maritima at 2.3 Å resolution

The expression, purification, crystallization, and structure determination of NAD-kinase from T. maritima are reported. Similarity to other NAD-kinases as well as homo-oligomrization state of the enzyme from T. maritima are discussed.

Structure at 1.6 Å resolution of the protein from gene locus At3g22680 from Arabidopsis thaliana

The crystal structure of the 18 kDa At3g22680 gene product from A. thaliana was determined at 1.6 Å resolution. At3g22680 shows no structural homology to any other known proteins and represents a new fold in protein conformational space.

Crystallization of the C-terminal globular domain of avian reovirus fibre

Partial proteolysis of the avian reovirus cell-attachment protein σC yields a major homotrimeric C-terminal fragment that presumably contains the receptor-binding domain. This fragment has been crystallized in the presence and absence of zinc sulfate and cadmium sulfate. One of the crystal forms diffracts synchrotron X-rays to 2.2–2.3 Å.

Lipopolysaccharide stabilizes the crystal packing of the ABC transporter MsbA

The use of lipopolysaccharide in the crystallization of the integral membrane protein MsbA was critical to the overall stability of the crystals and led to an increase in diffraction resolution.

Crystallization and preliminary X-ray analysis of a truncated mutant of yeast nuclear thiol peroxidase, a novel atypical 2-Cys peroxiredoxin

A double mutant of yeast nuclear thiol peroxidase has been crystallized in a truncated form. The crystal belongs to space group P3₂, with unit-cell parameters a = b = 37.54, c = 83.26 Å. A diffraction data set has been collected to 1.8 Å resolution.

Expression, purification and crystallization of the C-terminal domain of Escherichia coli adenylyltransferase

The C-terminal domain of adenylyltransferase (ATase) from Escherichia coli has been overexpressed, purified and crystallized in a form suitable for structure analysis.

Crystallization and X-ray crystallographic analysis of human STAT1

Human STAT1 (1–683) has been crystallized in the presence of a receptor-derived phosphopeptide. A diffraction data set has been collected and processed to 3.0 Å resolution.

Purification, crystallization and preliminary X-ray diffraction studies of the three components of the toluene 2,3-dioxygenase enzyme system

All three components of the toluene dioxygenase system have been expressed, purified and crystallized.

Purification, crystallization and preliminary X-ray diffraction studies on human Ca²⁺-binding protein S100B

Human recombinant EF-hand Ca²⁺-binding protein S100B has been purified and crystallized. A complete data set was recorded to 1.9 Å.

Expression, purification, crystallization and preliminary X-ray crystallographic studies of a novel acetylcitrulline de­acetylase from Xanthomonas campestris

The expression, purification and preliminary X-ray diffraction studies of a novel N-acetyl-L-citrulline deacetylase from X. campestris are reported.

Cloning, purification, crystallization and preliminary structural studies of penicillin V acylase from Bacillus subtilis

An unannotated protein reported from B. subtilis has been expressed in E. coli and identified as possessing penicillin V acylase activity. The crystallization and preliminary crystallographic analysis of this penicillin V acylase is presented.

Characterization of crystals of the Hjc resolvase from Archaeoglobus fulgidus grown in gel by counter-diffusion

The Holliday junction-cutting enzyme Hjc from A. fulgidus was crystallized by the counter-diffusion method in agarose gel and complete data were collected at 2.7 Å resolution using synchrotron radiation.

Crystallization and preliminary X-ray diffraction analysis of mouse 3(17)α-hydroxysteroid de­hydrogenase

Orthorhombic crystals of mouse 3(17)α-hydroxysteroid dehydrogenase were obtained from buffered polyethylene glycol solutions. The crystals diffracted to a resolution of 1.8 Å at the Swiss Light Source beamline X06SA.

Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestris

A conserved hypothetical protein XC1692 from X. campestris pv. campestris has been overexpressed in E. coli. The purified recombinant protein crystallized in a variety of forms and diffracted to a resolution of at least 1.45 Å.

Cloning, purification, crystallization and preliminary X-ray analysis of XC229, a conserved hypothetical protein from Xanthomonas campestris

A conserved hypothetical protein XC229 from X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. A crystal of the purified recombinant protein diffracted to a resolution of 1.80 Å.

A putative polyketide-synthesis protein XC5357 from Xanthomonas campestris: heterologous expression, crystallization and preliminary X-ray analysis

A putative polyketide-synthesis protein XC5357 from X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. The crystals diffracted to a resolution of at least 1.85 Å.

Preparation, crystallization and preliminary X-ray analysis of XC2382, an ApaG protein of unknown structure from Xanthomonas campestris

A putative ApaG gene product from X. campestris pv. campestris was overexpressed in E. coli, purified and crystallized. The crystals diffracted to a resolution of at least 2.3 Å.

Cloning, purification crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC6422 from Xanthomonas campestris

A conserved hypothetical protein XC6422 from X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. Crystals obtained from the purified recombinant protein showed a variety of forms that diffracted to at least 1.6 Å resolution.

Cloning, expression, crystallization and preliminary X-ray analysis of a putative multiple antibiotic resistance repressor protein (MarR) from Xanthomonas campestris

A putative repressor for the multiple antibiotic resistance operon from a plant pathogen X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. The crystals diffracted to 2.3 Å with good quality.

Crystallization and X-ray analysis of 2-de­oxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics

The crystallization of 2-deoxy-scyllo-inosose synthase, the key enzyme in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics, is reported.

Crystallization and preliminary X-ray diffraction study of BchU, a methyltransferase from Chlorobium tepidum involved in bacterio­chlorophyll c biosynthesis

Recombinant BchU from C. tepidum has been crystallized. Crystals diffract to 2.27 Å using synchrotron radiation at SPring-8 and belong to space group P6₁22 or P6₅22, with unit-cell parameters a = b = 81.5, c = 250.7 Å.

X-ray diffraction analysis of a crystal of HscA from Escherichia coli

A truncated form of HscA (52 kDa) containing both nucleotide- and substrate-binding domains has been crystallized and analyzed by X-ray diffraction. The crystal belongs to space group P2₁2₁2₁ and diffracts to 2.9 Å.

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapB (Rv2773c) from Mycobacterium tuberculosis

M. tuberculosis dihydrodipicolinate reductase, the enzyme that catalyzes the second committed step of lysine biosynthesis, has been cloned, expressed, purified and crystallized in three different crystal forms.