Cloning, sequence and crystallographic structure of recombinant iron superoxide dismutase from Pseudomonas ovalis

The gene encoding iron superoxide dismutase from P. ovalis has been cloned and sequenced; the recombinant enzyme has been crystallized and its structure determined.

Structure of XynB, a highly thermostable β-1,4-xylanase from Dictyoglomus thermophilum Rt46B.1, at 1.8 Å resolution

The structure of a highly thermostable family II xylanase has been determined at 1.8 Å resolution. Thermostability is attributed to increased polar surface and increased hydrogen bonding.

Structure of the C123S mutant of dienelactone hydrolase (DLH) bound with the PMS moiety of the protease inhibitor phenylmethylsulfonyl fluoride (PMSF)

The structure of the DLH (C123S) with PMS bound indicates that the reason the enzyme is able to catalyse a wide range of dissimilar substrates is a consequence of its capacity to undergo a coordinated restructuring of the active site and associated regions of the molecule without compromising the stability of its tertiary fold.

Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II

The structures of recombinant wild-type human acetylcholinesterase and of its E202Q mutant, as complexes with fasciculin-II, a `three-finger' snake neurotoxin, have been determined to 2.8 and 2.7 Å resolution, respectively. The overall structures of these complexes are similar to those of the Torpedo and mouse enzymes with fasciculin-II. Comparison of the wild-type and the mutant structures shows that removal of the charged group from the protein core, and its substitution by a neutral isosteric moiety, does not disrupt the functional architecture of the active center.

Structure of human α-thrombin complexed with RWJ-51438 at 1.7 Å: unusual perturbation of the 60A–60I insertion loop

The three-dimensional structure of the ternary complex consisting of human α-thrombin, hirugen and the active-site inhibitor RWJ-51438 has been determined at 1.7 Å resolution.

The atomic resolution structure of bucandin, a novel toxin isolated from the Malayan krait, determined by direct methods

The structure of bucandin, a novel three-finger toxin, has been determined by direct methods. The full-matrix least-squares refinement to atomic resolution, with anisotropic temperature factors, converged to an R factor of 12.4%.

Crystallographic studies of the interaction between the ferredoxin-NADP⁺ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule

The first structure of a complex between ferredoxin-NADP⁺ reductase and ferredoxin has been solved at 2.4 Å resolution by molecular replacement, anomalous dispersion and R_min search methods. The crystal was treated as a merohedral twin.

Single-wavelength anomalous diffraction phasing revisited

Analyzing the anomalous diffraction from seven different selenomethionine-labelled crystals, we show that the combination of single-wavelength anomalous-diffraction phasing and solvent flattening is sufficient to unambiguously determine most structures.

Evaluation of phase accuracy via topological and geometrical analysis of electron-density maps

A systematic analysis of local and global protein electron-density map properties is used to derive an empirical function to measure the average error in diffraction phase sets.

Evaporative microdialysis: an effective improvement in an established method of protein crystallization

Slow evaporation of the reservoir in microdialysis can lead to a significant increase in the crystal size of proteins for which the crystallization region of supersaturation is particularly limited.

Crystallization and preliminary crystallographic study of an extremophile cytochrome c₄ from Thiobacillus ferrooxidans

The acidic cytochrome c₄ from T. ferrooxidans has been cloned, expressed, purified and crystallized. The MAD method using the four Fe per asymmetric unit is used to solve the protein structure.

Crystallization and preliminary X-ray diffraction analysis of a eumenine mastoparan toxin: a new class of mast-cell degranulating peptide in the wasp venom

The crystallization and preliminary X-ray analysis of a mastoparan peptide isolated from the venom of the solitary wasp A. flavomarginatum micado is reported.

Preliminary crystallographic studies of an extremely thermostable KDG aldolase from Sulfolobus solfataricus

The growth of three crystal forms of 2-keto-3-deoxygluconate aldolase from the hyperthermophilic archaeon S. solfataricus is reported.

Crystallization and preliminary X-ray diffraction analysis of a recombinant cysteine-free mutant of crmA

The first crystallization of a serpin that is either viral or a cysteine proteinase inhibitor is described.

Crystallization and preliminary X-ray analysis of glucose de­hydrogenase from Bacillus megaterium IWG3

Glucose dehydrogenase from B. megaterium IWG3 has been crystallized and 1.7 Å resolution data have been collected using a synchrotron-radiation source.

Crystallization and preliminary X-ray crystallographic studies of response regulator for cyanobacterial phytochrome, Rcp1

The key response regulator of light regulation, Rcp1, from Synechocystis sp. has been crystallized in a form suitable for X-ray diffraction studies. The crystals belong to space group P6₃ and diffracted to 2.5 Å.

Expression, crystallization and preliminary X-ray diffraction studies of recombinant Bacillus anthracis lethal factor

The lethal factor (LF) produced by toxigenic strains of B. anthracis is a Zn-endopeptidase responsible of the lethal effects of anthrax. LF has been expressed in E. coli as recombinant GST fusion, purified and crystallized; preliminary crystallographic studies are described.

Crystallization and preliminary X-ray diffraction analysis of a functional form of pneumolysin, a virulence factor from Streptococcus pneumoniae

Crystals of a functional form of pneumolysin, a virulence factor of S. pneumoniae, have been obtained in complex with its activator, a cholesterol molecule, by the vapor-diffusion method. The crystallization process as well as the preliminary X-ray analysis are discussed.

Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the multidrug transporter activation protein (MtaN) from Bacillus subtilis

The DNA-binding domain of the MerR family member MtaN has been crystallized in space group I2₁2₁2₁. Intensity data have been collected from these crystals at 100 K at a synchrotron-radiation source to 2.75 Å resolution.

Crystallization and preliminary X-ray analysis of full-length annexin I comprising the core and N-terminal domain

Annexin I, a member of the annexin family of Ca²⁺- and phospholipid-binding proteins, has been crystallized with the complete N-terminus.

Crystallization and preliminary X-ray analysis of a bacterial lysozyme produced by Streptomyces globisporus

A bacterial lysozyme produced by S. globisporus was crystallized in space group P4₁2₁2, with unit-cell parameters a = 63.11, c = 121.1 Å. A clear molecular-replacement solution was obtained and the structure refinement is in progress.

Expression, purification and crystallization of human tau-protein kinase I/glycogen synthase kinase-3β

Full-length human tau-protein kinase I (TPK-I; also known as glycogen synthase kinase-3β, GSK-3β) was produced in E. coli and crystallized. The crystals diffract up to 2.3 Å resolution and belong to the orthorhombic space group , with unit-cell parameters a = 82.9, b = 86.1, c = 178.1 Å measured at 100 K.

Crystallization and preliminary crystallographic studies of trichomaglin, a novel ribosome-inactivating protein

Trichomaglin has been crystallized in two crystal forms.

Crystallization and preliminary X-ray analysis of CTLA-4 (CD152) membrane-external domain

The membrane-external domain of the immune modulator CTLA-4 (CD152) has been crystallized; the crystals diffract to 2.7 Å resolution at synchrotron sources.

Crystallization and preliminary X-ray crystallographic studies of the thermoactive pullulanase type I, hydrolyzing α-1,6 glycosidic linkages, from Fervidobacterium pennivorans Ven5

F. pennivorans Ven5 pullulanase type I was crystallized in the presence of the inhibitor β-cyclodextrin. The crystals belong to space group P2₁2₁2₁, with unit-cell parameters a = 76.8, b = 96.2, c = 98.5 Å, diffract to 2.2 Å using synchrotron radiation and contain one monomer in the asymmetric unit.

Crystallization and preliminary X-ray crystallographic studies on the bacteriophage Φ6 RNA-dependent RNA polymerase

Native and selenomethionyl-labelled RNA-dependent RNA polymerase from bacteriophage Φ6 crystallizes in space groups P2₁ and P3₁/P3₂. Data have been collected for both space groups to better than 3 Å resolution.

Crystallization and preliminary X-ray analysis of the auxin receptor ABP1

Monoclinic crystals of the maize auxin receptor ABP1 diffract to 1.9 Å resolution.

Purification, crystallization and preliminary X-ray crystallographic analysis of human CCG1-interacting factor B

Preliminary crystal data have been obtained for the first time for human CCG1-interacting factor B. The results of preliminary X-ray diffraction are discussed.

Crystallization and preliminary X-ray diffraction studies of a new crystal form of human secretory type IIA phospholipase A₂

Preliminary crystal data have been obtained for a new crystal form of human secretory phospholipase A₂ IIA crystallized with pentapeptide inhibitors. The enzyme crystallizes in space group C2, with unit-cell parameters a = 140.8, b = 38.9, c = 109.1 Å, β = 125.1°.

Nucleoside diphosphate kinase from the hyperthermophilic archaeon Methanococcus jannaschii: overexpression, crystallization and preliminary X-ray crystallographic analysis

Nucleoside diphosphate kinase from M. jannaschii has been crystallized using polyethylene glycol 4000 as precipitant. Native data have been collected to 2.30 Å resolution using synchrotron X-rays.

Purification, crystallization and preliminary X-ray crystallographic analysis of ATP-phosphoribosyltransferase from Escherichia coli

Crystals of ATP-phosphoribosyltransferase from E. coli were obtained by the vapour-diffusion method and diffract to 2.7 Å. The quaternary structure is determined based on the preliminary crystallographic studies.

Preliminary X-ray diffraction studies of rabbit muscle triose phosphate isomerase (TIM)

Here the crystallization, data collection and molecular-replacement solutions obtained for two crystalline forms of triose phosphate isomerase, one determined at 85 K and the other at 298 K are reported.

Cloning, expression, purification and crystallization of di­hydroxybutanone phosphate synthase from Magnaporthe grisea

Dihydroxybutanone phosphate synthase from M. grisea was cloned, expressed and crystallized. Crystals diffract to 1.0 Å resolution.

Crystallization and preliminary X-ray studies of oligandrin, a sterol-carrier elicitor from Pythium oligandrum

Oligandrin, a small 10 kDa phytotoxin with sterol-carrier properties, has been crystallized from PEG 4000 at pH 4.5.

The purification, crystallization and preliminary structural characterization of glucose-1-phosphate thymidylyltransferase (RmlA), the first enzyme of the dTDP-L-rhamnose synthesis pathway from Pseudomonas aeruginosa

The anabolism of L-rhamnose in many pathogenic bacteria presents itself as a possible novel therapeutic target. RmlA is the first of the four enzymes involved in this pathway. Crystallization and preliminary structural characterization are reported.

Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome

A new E. coli L-asparaginase belonging to the class of Ntn hydrolases has been crystallized in the orthorhombic space group P2₁2₁2₁. The crystals diffract to 1.65 Å resolution and contain an (αβ)₂ heterotetramer in the asymmetric unit, where the subunits α and β are the product of autocatalytic cleavage of the immature protein.

Purification, crystallization and preliminary diffraction study of β-galactosidase from Penicillium sp.

β-galactosidase from Penicillium sp. was crystallized and diffracted to 1.85 Å resolution. It belonged to the tetragonal P4₃(P4₁) space group, with unit-cell parameters a = b = 110.82, c = 161.28 Å.

Apotheosis, not apocalypse: methods in protein crystallography

Report of the workshop Toward Automation of Structure Determination in Macromolecular Crystallography held on 20–21 June 1999.

Crystallization and preliminary X-ray diffraction studies of monomeric isocitrate de­hydrogenase from Corynrbacterium glutamicum. Erratum

An erratum to Acta Cryst. (1999), D55, 1584–1585.

Crystallization and preliminary X-ray analysis of the conserved domain IV of Escherichia coli 4.5S RNA. Erratum

An erratum to Acta Cryst. (2000), D56, 1033–1037.