A recently published crystallographic model of GspB in complex with a disaccharide was proposed to provide insight into the interaction of the S. gordonii adhesin with the cell sialyl-T antigen from host cells. However, a close inspection of this model revealed that in this complex a buffer molecule was mistaken for the disaccharide. As a consequence, this complex provides no information regarding the interaction of GspB with host cell receptors.
The 155 amino-acid FP domain of the human F-box protein Fbxo7 was successfully expressed in bacteria, purified and crystallized. Native and single-wavelength anomalous dispersion data sets have been collected.
The cloning, expression and purification of different fragments of the S. pyogenes SpyCEP protein are reported. Preliminary X-ray diffraction analysis of a 1580-residue selenomethionine-labelled ectodomain fragment is described.
The C-terminal RNA recognition motif of human ETR-3 protein involved in myotonic dystrophy was over-expressed, purified and crystallized. The crystals obtained diffracted X-rays to 3 Å resolution and belonged to space group P213.
The GH42 β-galactosidase GanB from G. stearothermophilus has been crystallized in the primitive orthorhombic space group P212121. Complete diffraction data sets have been measured for the wild-type enzyme (2.45 Å resolution) and its catalytic mutant (E323A; 2.50 Å resolution) for use in a full three-dimensional structural analysis of the GanB protein.
Peptide deformylase catalyzes the deformylation of N-formylated methionine in newly synthesized polypeptides in prokaryotes and some eukaryotic organelles. The synthetic codon-optimized def gene from C. jejuni was cloned and the protein expressed, purified and crystallized. A preliminary X-ray crystallography analysis of the C. jejuni peptide deformylase crystals was performed.
A proteolytically stable fragment of a plasmid replication initiation protein from the thermophile G. stearothermophilus has been biochemically characterized, crystallized and diffraction data collected to a resolution of 2.5 Å.
A putative xylose isomerase from B. thetaiotaomicron has been crystallized (space group P1, unit-cell parameters a = 96.3, b = 101.7, c = 108.3 Å, α = 82.8, β = 68.2, γ = 83.0°). Diffraction data have been collected to 2.10 Å resolution using synchrotron X-rays.
The C-terminal domain of the fibre protein from turkey adenovirus 3, a siadenovirus, consisting of amino acids 304–454, has been crystallized. Diffraction data were obtained to 2.0 and 2.14 Å resolution for a native crystal and a selenomethionine-derivative crystal, respectively.
A (2R,3R)-2,3-butanediol dehydrogenase from B. coagulans 2-6 was expressed in E. coli BL21 (DE3) and purified. Crystallization and preliminary X-ray crystallographic analysis were performed for this recombinant enzyme.
A phosphate-binding protein endowed with phosphatase activity, previously dubbed LapA, from P. aeruginosa PAO1 has been crystallized. The crystals diffracted to 0.87 Å resolution and belonged to space group P21.
Cellobiose 2-epimerase epimerizes and isomerizes β-1,4- and α-1,4-gluco-oligosaccharides. The cellobiose 2-epimerase gene from D. turgidum was cloned and the protein was expressed, purified and crystallized. A preliminary X-ray crystallography analysis of the cellobiose 2-epimerase crystals was performed.
The two Plasmodium actin isoforms were expressed, purified and crystallized in complex with the gelsolin G1 domain. Crystals diffracting to high resolution were obtained and data sets for actin I and II were collected to 1.19 and 2.2 Å resolution, respectively.
Dihydrodipicolinate synthase (DHDPS) catalyses the rate-limiting step in the biosynthesis of meso-diaminopimelate and lysine. Here, the cloning, expression, purification and crystallization of DHDPS from the intracellular pathogen Legionella pneumophila are described.