Crystal structure of small protein crambin at 0.48 Å resolution

A protein crystallographic data collection using the PETRA II source sets the record in crystallographic resolution for a biological macromolecule (0.48 Å) for the small protein crambin and increases available data for refinement by a factor of 1.5. The quality of the data collected is evident by comparing the merging R factor between two different crambin data sets, collected from different crystals and using different beamlines and protocols (6%) and the final crystallographic R factor of 12.7% for the model refinement.

Structural analysis of a putative family 32 carbohydrate-binding module from the Streptococcus pneumoniae enzyme EndoD

EndoD from S. pneumoniae is a large multimodular virulence factor that contains a putative carbohydrate-binding module (CBM). Here, the structure of the putative CBM is described.

Cocrystallization studies of full-length recombinant butyrylcholinesterase (BChE) with cocaine

The cocrystallization of recombinant full-length human BChE with cocaine yields a 3.0 Å resolution structure of the complex with the hydrolysis product benzoic acid. The benzoate is positioned in the acyl cavity, where it appears to forms a hydrogen bond to the active-site Ser.

Structure of a mutant β toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility

The structure of a mutant β toxin from S. aureus in which a hydrophobic β-hairpin has been deleted shows unanticipated domain swapping leading to the formation of conformationally flexible dimers.

The role of Co²⁺ in the crystallization of human SENP1 and comments on the limitations of automated refinement protocols

Crystallographic analysis of the human SENP1 catalytic domain identified a well ordered Co²⁺ ion that contributes to intermolecular interactions relevant to crystallization of the enzyme. The presence of this ion was overlooked in previous studies.

Structure of Francisella tularensis peptidyl-tRNA hydrolase

The structure of peptidyl-tRNA hydrolase from F. tularensis, the causative agent of tularemia, is comparable to that of other bacterial peptidyl-tRNA hydrolases, with most residues in the active site conserved amongst the family. The resultant reagents, structural data, and analyses provide essential information for structure-based design of novel inhibitors for this class of proteins.

Crystallization and preliminary X-ray crystallographic analysis of human autotaxin

The α isoform of human autotaxin has been crystallized. Diffraction data were collected to 3.0 Å resolution using synchrotron radiation.

Crystallization and initial crystallographic analysis of AafA: the major adhesive subunit of the enteroaggregative Escherichia coli AAF/II pilus

The Enteroaggregative Escherichia coli AAF/II pilus plays an important role in the attachment to and invasion of the host during the initial stages of colonization. Here, the major adhesive subunit of AAF/II has been crystallized at pH 3.4 and diffraction data have been collected to 2.1 Å resolution.

Crystallization and preliminary X-ray crystallographic studies of the CIDE-domain complex between Drep2 and Drep3 from Drosophila melanogaster

In this study, the CIDE domains of Drep2 and Drep3 from Drosophila melanogaster were purified in Escherichia coli, after which they formed a stable complex in vitro and were crystallized by the hanging-drop vapour-diffusion method.

Cloning, purification, crystallization and preliminary crystallographic analysis of the human histone de­acetylase sirtuin 1

The human histone deacetylase sirtuin 1 was expressed and purified. Crystals were obtained and diffracted to 3.45 Å in space group P622.

Crystallization and preliminary X-ray analysis of the bacillaene synthase trans-acting acyltransferase PksC

The expression, purification and crystallization of the trans-acting acyltransferase PksC from the bacillaene hybrid polyketide synthase/nonribosomal peptide synthetase is described. The crystals belonged to the orthorhombic space group P2₁2₁2₁ and diffracted to 1.44 Å resolution.

Expression, crystallization and preliminary X-ray data analysis of NT-Als9-2, a fungal adhesin from Candida albicans

Details of the expression and crystallization of the N-terminal fragment of Als9-2, an adhesin from the human commensal/pathogenic fungus C. albicans, are reported. Preliminary analysis of the collected X-ray data is also discussed.

Cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of an inositol monophosphatase family protein (SAS2203) from Staphylococcus aureus MSSA476

The cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of an inositol monophosphatase family protein (SAS2203) from S. aureus MSSA476 is reported.

A rational protocol for the successful crystallization of L-amino-acid oxidase from Bothrops atrox

L-Amino-acid oxidase from B. atrox has been crystallized by combining seeding with oil modulation of vapour equilibration. A complete data set has been collected to 2.3 Å resolution from a native crystal.

Purification, crystallization and preliminary X-ray diffraction analysis of ThiM from Staphylococcus aureus

5-(Hydroxyethyl)-4-methylthiazole kinase from S. aureus, which is essential to vitamin B₁ metabolism, has been crystallized in space group P1. The crystals diffracted to 2.1 Å resolution.

Cloning, expression and preliminary crystallographic analysis of the equine infectious anaemia virus (EIAV) gp45 ectodomain

The equine infectious anaemia virus gp45 ectodomain was cloned, expressed and crystallized. Preliminary crystallographic analysis showed that the protein belonged to space group P6₃ and contained one molecule per asymmetric unit.

Purification, crystallization and preliminary X-ray crystallographic analysis of a central domain of human splicing factor 1

This work describes the expression, purification, circular dichroism spectrum and crystallization of a central domain from human Splicing Factor 1. A native, 2.5 Å resolution data set is reported.

Overproduction, purification, crystallization and preliminary X-ray characterization of a novel carbohydrate-binding module of endoglucanase Cel5A from Eubacterium cellulosolvens

The novel N-terminal carbohydrate-binding module of the family 5 glycoside hydrolase endoglucanase Cel5A from E. cellulosolvens has been crystallized and MAD data have been collected to 1.75 Å resolution.

Crystallization and preliminary X-ray diffraction studies of the catalytic domain of a novel chitinase, a member of GH family 23, from the moderately thermophilic bacterium Ralstonia sp. A-471

The catalytic domain of a novel chitinase, which is a member of GH family 23, from the moderately thermophilic bacterium Ralstonia sp. A-471 was crystallized and diffraction data were collected to 1.85 Å resolution.

Crystallization and diffraction analysis of β-N-acetylhexosaminidase from Aspergillus oryzae

The fungal β-N-acetylhexosaminidase from A. oryzae was crystallized and diffraction data were collected from two crystal forms to 3.2 and 2.4 Å resolution, respectively.

Crystallization and preliminary X-ray crystallographic analysis of CheW from Thermotoga maritima: a coupling protein of CheA and the chemotaxis receptor

CheW from T. maritima has been crystallized (space group P6₃, unit-cell parameters a = b = 61.265, c = 361.045 Å). Diffraction data have been collected to 3.1 Å resolution using synchrotron X-ray radiation.

Crystallization and preliminary X-ray diffraction analysis of recombinant chlorocatechol 1,2-dioxygenase from Pseudomonas putida

Recombinant chlorocatechol 1,2-dioxygenase from P. putida has been crystallized in the presence of polyethylene glycol as the precipitant agent and magnesium acetate as an additive. The structure was solved by the MR-SAD approach.

Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of human ribosomal protein L7a (RPL7a)

The N-terminal domain of the human ribosomal protein L7a (RPL7a) was crystallized. The crystals were found to belong to the tetragonal space group P4₁22 or P4₃22, with unit-cell parameters a = 92.28, b = 92.28, c = 236.59 Å. The crystals were obtained at 293 K and diffracted to a resolution of 3.5 Å.

Purification, crystallization and preliminary X-ray crystallographic analysis of a methanol de­hydrogenase from the marine bacterium Methylophaga aminisulfidivorans MP^T

In order to obtain molecular insights into the methanol-oxidizing system of M. aminisulfidivorans, a native heterotetrameric α₂β₂ methanol dehydrogenase complex was directly purified from M. aminisulfidivorans MP^T grown in the presence of methanol and crystallized.

Expression, purification and crystallization of the Cmi immunity protein from Escherichia coli

The colicin M immunity protein Cmi protects E. coli cells against killing by colicin M. The Cmi protein was produced for structure determination and crystals were obtained which diffracted to high resolution.

Crystallization and preliminary X-ray diffraction analysis of cyclic imide hydrolase (CIH) from Pseudomonas putida YZ-26

A recombinant cyclic imide hydrolase from P. putida YZ-26 has been crystallized by the hanging-drop method. This will be helpful in understanding the role of CIH in pyrimidine metabolism and organic acid bioconversion.

Crystallization and preliminary X-ray diffraction analysis of a galactose-specific lectin from the seeds of Butea monosperma

A galactose specific lectin was purified from the seeds of a tropical tree, Butea monosperma. Its X-ray structure was solved by molecular replacement.