Structure of human erythrocyte NADH-cytochrome b₅ reductase

The structure of human NADH-cytochrome b₅ reductase at 1.75 Å resolution is the same as that of rat NADH-cytochrome b₅ reductase except for a large main-chain shift caused by a Pro268Thr substitution. Five mutations seem to be related to cytochrome b₅.

Recurring main-chain anion-binding motifs in short polypeptides: nests

Peptidic molecules in the CSD are searched for nests, three-amino-acid residue anion-binding motifs found commonly in proteins. 37 are found. One, in the antibiotic vancomycin, has the function of binding the C-terminal carboxylate group of the bacterial cell wall precursor peptide.

Inhibitor binding at the protein interface in crystals of a HIV-1 protease complex

In the course of investigating the complex of HIV-1 protease with a novel phenylnorstatine inhibitor, two inhibitor molecules were found to be bound to the enzyme, one in a non-productive mode. The contribution of the contacts of this inhibitor molecule at the protein interface to the crystal quality is discussed.

Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase from Shewanella oneidensis at 1.6 Å: identification of farnesyl pyrophosphate trapped in a hydrophobic cavity

The structure of 2C-methyl-D-erythritol-2,4-­cyclophosphate from S. oneidensis MR1 (SO3437) has been determined to 1.6 Å resolution in the absence of substrate.

Radiation-damage-induced phasing with anomalous scattering: substructure solution and phasing

The effects of radiation damage on iodinated thaumatin crystals have been analysed. It was shown that combination of the anomalous and isomorphous signals in the form of RIPAS (radiation-damage-induced phasing with anomalous scattering) is beneficial for both locating the substructure and subsequent phasing.

Structure determination and refinement at 2.44 Å resolution of argininosuccinate lyase from Escherichia coli

The crystal structure of E. coli argininosuccinate lyase has been determined at 2.44 Å resolution; in this structure, one active site, complexed with two phosphate ions, adopts the closed conformation.

Solution and structure of an alternating D,L-peptide

The D,L-alternating peptide H-(L-Tyr-D-Tyr)₄-L-Lys-OH adopts a gramicidin A-like structure. Fragment-search strategies aiming to exploit the high-resolution data available (1.3 Å) were tested.

A pivotal role for reductive methylation in the de novo crystallization of a ternary complex composed of Yersinia pestis virulence factors YopN, SycN and YscB

De novo crystallization of a ternary complex composed of Y. pestis virulence factors YopN, SycN, and YscB could only be achieved after reductive methylation of surface-exposed lysine residues. This case study also demonstrates that the modification can be safely employed on multiprotein complexes and selenomethionine-substituted samples, underscoring its general potential as a crystallization tool, even in high-throughput settings.

Optimizing the error term in direct-method SAD phasing

The influence of the error term on direct-method SAD phasing is examined. A method for automatically tuning the scaling factor in the error term is proposed.

Direct-method SAD phasing with partial-structure iteration: towards automation

Structure fragments resulting from automatic model building based on initial direct-method SAD phasing are fed back to the direct-method probability formula in order to strengthen the phasing power and to benefit the automation of structure solution of proteins.

Structure of the RNA-processing inhibitor RraA from Thermus thermophilis

The X-ray crystallographic structure of T. thermophilis RraA has been solved to 2.3 Å resolution.

Crystallization and preliminary X-ray crystallographic analysis of chorismate synthase from Mycobacterium tuberculosis

The last step of the shikimate pathway is catalyzed by chorismate synthase (CS). Optimization of crystallization trials allowed the crystallization of homogeneous recombinant CS from M. tuberculosis.

Crystallization and preliminary X-ray diffraction analysis of homing endonuclease I-Tsp061I

A thermostable homing endonuclease from Thermoproteus sp. IC-061 has been crystallized. The crystals diffract to 2.7 Å resolution.

Cloning, expression, purification, crystallization and preliminary X-ray characterization of the full-length single-stranded DNA-binding protein from the hyperthermophilic bacterium Aquifex aeolicus

The full-length single-stranded DNA-binding protein (SSB) from the extremophile A. aeolicus has been expressed in Escherichia coli, purified and crystallized and initial X-ray data have been obtained.

Crystallization and preliminary crystallographic analysis of the fusion core of the spike protein of the murine coronavirus mouse hepatitis virus (MHV)

Preliminary crystallographic data of the fusion core of the spike protein of the murine coronavirus mouse hepatitis virus have been obtained.

Crystallization and preliminary X-ray crystallographic analysis of chitinase F1 (ChiF1) from the alkaliphilic Nocardiopsis sp. strain F96

Crystals of ChiF1 have been grown and they diffract beyond 1.24 Å resolution.

Expression, purification, crystallization and preliminary X-ray diffraction studies of human liver regucalcin

Human liver regucalcin, consisting of 299 amino-acid residues, has been overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion method in the presence of polyethylene glycol 4000 as a precipitant.

Crystallization and preliminary X-ray analysis of VCBP3 from Branchiostoma floridae

VCBP3, an immunoglobulin-like protein from the protochordate B. floridae with the characteristics of a `primordial' antigen receptor, has been crystallized and complete native data sets have been collected to 2.4 Å resolution. Isomorphous crystals from two different crystallization conditions are consistent with space groups P3₁21 and P3₂21, with unit-cell parameters a = b = 58.99, c = 79.21 Å, α = β = 90, γ = 120°.

Crystallization and preliminary diffraction studies of TraF, a component of the Escherichia coli type IV secretory system

The expression, purification, crystallization and preliminary X-ray diffraction studies of the protein TraF from the E. coli F plasmid are reported.

Purification, crystallization and preliminary crystallographic studies of the ligand-binding domain of a plant vacuolar sorting receptor

Vacuolar sorting receptor (VSR) proteins target ligands to the lytic vacuole in a sequence-specific manner. Purification from Drospohila S2 cells, crystallization and preliminary X-ray diffraction studies of Arabidopsis thalia VSR, AtBP80b, have been carried out.

Expression, purification and preliminary X-ray analysis of crystals of Bacillus subtilis glutamate racemase

Glutamate racemase from B. subtilis has been crystallized in the presence of L-glutamate in a form suitable for structure determination.

Purification, characterization, crystallization and preliminary X-ray crystallographic analysis of two novel C-type lectin-like proteins: Aall-A and Aall-B from Deinagkistrodon acutus venom

Aall-A and Aall-B, two novel heterodimeric snake-venom C-type lectin-like proteins (sv-CLPs), were purified from the venom of D. acutus from Anhui, China, and crystallized.

Crystallization and preliminary X-ray crystallographic studies of a lectin from the mushroom Marasmius oreades

The M. oreades agglutinin (MOA) has been crystallized. Crystals diffract anisotropically to 2.5 Å resolution. A complete X-ray data set has been obtained to 3.0 Å resolution.

Expression, crystallization and preliminary structural analysis of the ectoplasmic region of apical membrane antigen 1 from Plasmodium vivax, a malaria-vaccine candidate

The ectoplasmic region of apical membrane antigen 1 from P. vivax has been expressed and crystallized in two crystal forms. Phases have been obtained by the MAD technique using a Pt derivative.

Crystallization and preliminary analysis of a water-forming NADH oxidase from Lactobacillus sanfranciscensis

The water-forming NADH oxidase from L. sanfranciscensis has been crystallized in space group P2₁2₁2₁ and X-ray diffraction data to 1.85 Å resolution have been collected.

RARβ ligand-binding domain bound to an SRC-1 co-activator peptide: purification, crystallization and preliminary X-ray diffraction analysis

The retinoic acid receptor β ligand-binding domain has been expressed and crystallized bound to a synthetic retinoid (TTNPB) with or without a co-activator peptide (SRC-1).

Crystallization, data collection and phasing of infestin 4, a factor XIIa inhibitor

Crystals of infestin 4, a factor XIIa Kazal-type inhibitor from T. infestans, diffracted to 1.8 Å resolution and belong to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 25.89, b = 45.64, c = 57.41 Å.

Preparation, crystallization and preliminary X-ray analysis of a complex between the Plasmodium vivax sexual stage 25 kDa protein Pvs25 and a malaria transmission-blocking antibody Fab fragment

Crystals of the complex between the P. vivax sexual stage 25 kDa protein Pvs25 and a malaria transmission-blocking Fab diffract X-rays to 3.5 Å. Two complex molecules are predicted per asymmetric unit.

Purification, crystallization and preliminary X-ray analysis of mexicain

Mexicain, a cysteine protease, has been extracted from the latex of the tropical plant Pileusmexicanus, purified and crystallized. The crystals belong to the space group P2₁ and they diffract X-rays to 2.1 Å resolution.

Crystallization and preliminary X-ray analysis of pyridoxal 4-de­hydrogenase, the second enzyme in degradation pathway I of pyridoxine

Pyridoxal 4-dehydrogenase from Microbacterium luteolum has been crystallized by the sitting-drop vapour-diffusion method. The crystals were monoclinic and belonged to space group C2, with unit-cell parameters a = 107.0, b = 56.7, c = 130.2 Å, β = 103.6°. Diffraction data were collected from a single crystal to 2.0 Å.

Crystallization and atomic resolution X-ray diffraction of the catalytic domain of the large sialidase, nanI, from Clostridium perfringens

The catalytic domain of one of three sialidases encoded by the C. perfringens genome has been subcloned and crystallized. The diffraction of this 50 kDa domain to beyond 0.92 Å will allow detailed mechanistic enzymology of this enzyme superfamily.

Crystallization and preliminary X-ray diffraction analysis of spermidine synthase from Helicobacter pylori

The crystallization of spermidine synthase from H. pylori is reported.

Crystallization and preliminary X-ray analysis of sulfite de­hydrogenase from Starkeya novella

Sulfite dehydrogenase from S. novella has been crystallized. Crystals diffract to at least 1.8 Å resolution and belong to space group P2₁2₁2, with unit-cell parameters a = 97.5, b = 92.5, c = 55.9 Å.

Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase

Crystals of wild-type and two mutants of apo tryptophanase from E. coli belong to space group F222 and diffract to 1.9 Å.

Crystallization and preliminary X-ray diffraction studies of a protein di­sulfide oxidoreductase from Aquifex aeolicus

A protein disulfide oxidoreductase from A. aeolicus has been crystallized for the first time. Crystals belong to space group R32 and diffract to 2.4 Å resolution.

Crystallization of a core fragment of the flagellar hook protein FlgE

The hook is a short, highly curved segment of the bacterial flagellum, working as a universal joint, and is a helical assembly of about 120 copies of a single protein FlgE (42 kDa). The expression, purification, crystallization and diffraction data collection of a 31KDa fragment of FlgE, which is otherwise extremely difficult to crystallize because of its strong polymerization ability, are reported.

Crystallization and preliminary X-ray analyses of the active and the inactive forms of family GH-8 chitosanase with subclass II specificity from Bacillus sp. strain K17

Chitosanase from Bacillus sp. strain K17, which belongs to glycoside hydrolase family 8 and exhibits subclass II specificity, has been crystallized in two forms corresponding to the active and inactive states.

Crystallization and preliminary X-ray crystallographic studies of mouse autocrine motility factor

Mouse autocrine motility factor has been crystallized in the absence and presence of carbohydrate phosphate inhibitors. Diffraction data have been collected using synchrotron radiation.

Crystallization and preliminary X-ray analysis of a proteinase-K-resistant domain within the phosphoprotein of vesicular stomatitis virus (Indiana)

A stable domain of the vesicular stomatitis virus phosphoprotein was crystallized. The crystals belonged to space group P4₁2₁2 or P4₃2₁2, with unit-cell parameters a = b = 74.50, c = 156.84 Å, and diffraction data were collected to 2.75 Å.

Glutamate-5-kinase from Escherichia coli: gene cloning, overexpression, purification and crystallization of the recombinant enzyme and preliminary X-ray studies

The production and crystallization of recombinant E. coli glutamate-5-kinase, the enzyme that catalyzes the first and feedback-controlled step of proline biosynthesis and a member of the amino-acid kinase enzyme family, is reported. In addition to the catalytic machinery, this enzyme contains a PUA putative RNA-binding domain that endows it with gene-expression regulatory properties.

Crystallization and preliminary X-ray crystallographic studies of human 2′,3′-cyclic nucleotide 3′-phosphodiesterase

Crystals of the catalytic fragment of human 2′,3′-cyclic nucleotide 3′-phosphodiesterase (hCNP-CF) have been obtained. The crystals diffract X-rays to 1.8 Å resolution.

Crystallographic characterization of the N-terminal domain of PEX1

PEX1 N-terminal domain crystals have been prepared. The crystals belong to space group P3₁ or P3₂, with unit-cell parameters a = b = 63.5, c = 33.5 Å, and contain one protein molecule per crystallographic asymmetric unit. An intensity data set was collected to a resolution of 2.05 Å.

Purification, identification and preliminary crystallographic characterization of a novel seed protein from Vigna unguiculata

Purification, identification and preliminary crystallographic studies on an allergy-related protein from V. unguiculata seeds were carried out. The protein, crystals of which diffract to about 2.1 Å resolution, does not indicate homology with any protein with known crystal structure.

Purification, crystallization and preliminary X-ray structure analysis of the banana lectin from Musa paradisiaca

The banana lectin from M. paradisiaca has been purified and crystallized and the crystal structure studied.

Crystallization of a proteolyzed form of the horse pancreatic lipase-related protein 2: structural basis for the specific detergent requirement

A proteolyzed form of horse PLRP2 has been crystallized by the hanging-drop vapour-diffusion method in complex with DDAO. Native data have been collected to 2.9 Å resolution.

Structure of the phenazine biosynthesis enzyme PhzG

This work describes the structure of PhzG from two species of Pseudomonas.

SAD phasing by combination of direct methods with the SOLVE/RESOLVE procedure. Erratum

An erratum to the paper by Wang et al. (2004), Acta Cryst. D60, 1244–1253.