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The C-terminal domain of a bacteriophage P2 tail-spike protein, gpV, was crystallized and its structure was solved at 1.27 Å resolution. The refined model showed a triple β-helix structure and the presence of iron, calcium and chloride ions.
Structure-based identification and validation by protein X-ray crystallography of halomethyl ketone derivatives that inhibit caspase-3 without an aspartic acid in the P1 position is reported.
The crystal structure of the RuBisCO assembly chaperone RbcX from a thermophilic cyanobacterium has been determined at 1.7 Å resolution. The dimeric structure is capable of a hinge movement (probably connected with binding of the RuBisCO large subunit) pivoted on a kink in two long antiparallel α-helices.
The structure of a monomeric effector domain from influenza A virus NS1 is presented from diffraction data extending to 1.8 Å resolution. Comparison of this and other NS1 effector-domain structures shows conformational changes at a strand–strand packing interface, hinting at a role for β-strand augmentation in NS1 function.
Saxthrombin, a snake-venom thrombin-like enzyme from Gloydius saxatilis, was purified and crystallized to obtain a high-quality crystal, from which data were acquired to 1.43 Å resolution.
The crystal structure of the M. tuberculosis soluble inorganic pyrophosphatase Rv3628 determined at pH 7.0 reveals conformational changes compared with the structure at pH 5.0. The conformational changes arise not only as a consequence of the different pH but also of the presence of two potassium ions bound to the protein.
The structure of immunoglobulin-like repeat 10 from human filamin A solved at 2.44 Å resolution suggests the potential effects of mutations correlated with otopalatodigital syndrome spectrum disorders.
The p38αY323T active mutant crystallized in two different forms representing different structural features. It has been shown that the crystal profile and the resultant structures are biased by the source microseeds.
UDP-glucose-4-epimerase from A. nidulans has been crystallized as a complex with the substrate UDP-galactose using the microbatch method under paraffin oil.
Crystals of swine CD8α diffracted to 1.8 Å resolution and belonged to space group P3221, with unit-cell parameters a = 80.97, b = 80.97, c = 95.19 Å; they contained two molecules in the asymmetric unit. The Matthews coefficient and solvent content were calculated to be 3.23 Å3 Da−1 and 61.89%, respectively.
Crystals of 6-aminohexanoate-oligomer hydrolase have been obtained by the sitting-drop vapour-diffusion method using sodium citrate as a precipitant. Diffraction data for native and K2PtCl4-derivative crystals were collected to resolutions of 2.00 and 2.20 Å, respectively.
The PIG-S71–467 subunit of the yeast GPI transamidase complex was cloned, overexpressed, purified and crystallized. The crystals belonged to space group C2 and diffracted to 3.2 Å resolution.
BmooPLA2-I, an acidic, catalytic and nontoxic phospholipase A2 from B. moojeni venom that is able to inhibit platelet aggregation and induce a hypotensive effect, has been crystallized. An X-ray diffraction data set was collected to 1.6 Å resolution and a molecular-replacement solution was obtained.
Cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of a 12R-LOX–chaperone complex are reported. The crystals belonged to the space group P21 and diffracted to 4 Å resolution.
The expression, purification and crystallization of a PHD domain of human JARID1B are described.
β-Galactosidase from the psychrotrophic and halotolerant Planococcus sp. L4 (BgaP) was crystallized and a complete data set was collected. There are six protein subunits in the asymmetric unit.
Glucokinase from S. griseus (SgGlkA) was expressed, purified and crystallized using the sitting-drop vapour-diffusion method. A crystal of SgGlkA in complex with glucose diffracted X-rays to 1.84 Å resolution.
Thioredoxin reductase from S. coelicolor was crystallized and diffraction data were collected to 2.4 Å resolution.
The mimivirus L544 gene product was expressed in E. coli and crystallized; preliminary phasing of a MAD data set was performed using the selenium signal present in a crystal of recombinant selenomethionine-substituted protein.
The purification, crystallization and preliminary X-ray structure analysis of the laccase from G. lucidum are reported.
P. furiosus PF2050 has been crystallized. Diffraction data were collected to 1.56 Å resolution using synchrotron X-rays.
The small regulatory subunit of acetohydroxylate synthase (IlvH) from M. tuberculosis has been crystallized and preliminary crystallographic analysis has been performed.
The crystallization of PA3346RS from P. aeruginosa is reported.
Human Thrsp has been crystallized as a prelude to the determination of its three-dimensional structure by X-ray crystallography.
Human MutSβ is a 232 kDa heterodimer (MSH2–MSH3) involved in the lesion-recognition step of mismatch repair. Here, the overexpression, purification, biochemical characterization and cocrystallization of MutSβ with a duplex DNA substrate are reported.
Yeast tRNA-thiouridine modification protein 1 was overpressed in E. coli, purified and crystallized. The crystals belonged to space group I41 and diffracted to a resolution of 1.9 Å.
Lac15 from a marine microbial metagenome has been crystallized and preliminary crystallographic analysis has been performed.
O-Acetylhomoserine sulfhydrylase from M. tuberculosis H37Rv has been crystallized and preliminary X-ray crystallographic analysis has been performed.
The expression, purification and preliminary crystallographic analysis of CYP153C1, an alkane-binding cytochrome P450 enzyme, are reported.
To elucidate the mechanism of oxaloacetate decarboxylation by Cg1458, recombinant Cg1458 has been purified and crystallized.
Microfluidic crystallization using the Crystal Former improves the identification of initial crystallization conditions relative to screening via vapour diffusion.
An addendum to the article by Ahn et al. [Acta Cryst. (2011) F67, 689–691].
A correction to the article by Park et al. [(2011). Acta Cryst. F67, 800–802].