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The crystal structure of T. maritima tRNase Z has been determined at 1.97 Å. The structure shows the flexible arm and the fully metal-binding active site.
Hepatitis B virus capsids have significant potential as carriers for immunogenic peptides. The crystal structure of the T = 4 particle of hepatitis B core protein containing an N-terminal extension reveals that the fusion peptide is exposed on the exterior of the particle.
The X-ray crystallographic structure of the complement regulator CD59 at 1.15 Å resolution hints at modes of interaction with C8/C9.
Crystal structures of human recombinant calmodulin were determined in the presence of lead and barium ions.
The MafB transcription factor (residues 211–305) has been crystallized in complex with the 21 bp Cmare DNA-binding site. Native and mercury-derivatized data collection and preliminary analyses are reported.
Crystallization of the α2,6-sialyltransferase from Photobacterium.
A recombinant mutant (C47S) of cytosolic thioredoxin peroxidase 1 from S. cerevisiae was expressed, purified and crystallized by the hanging-drop vapour-diffusion method from protein previously treated with 1,4-dithiothreitol. The crystals belong to the monoclinic space group C2 and diffraction data were collected to 2.8 Å resolution using a synchrotron-radiation source.
The cloning, expression, purification and crystallization of recombinant human kallikrein 7, directly synthesized in the active form in E. coli, is described. Diffraction data were collected to 2.8 Å resolution from native crystals.
Diffraction-quality crystals of the apo (1.7 Å) and zinc-bound forms (2.2 Å) of the water-soluble C-terminal domain of the putative zinc transporter CzrB from T. thermophilus have been grown using recombinant production of the protein in E. coli and a combination of vapour-diffusion, batch and seeding crystallogenesis techniques.
Crystals of the cytosolic domain of the Mg2+ transporter MgtE from T. thermophilus in the presence and absence of Mg2+ diffracted X-rays to 2.3 and 3.5 Å resolution, respectively, and belong to space groups P6522 (a = b = 57.7, c = 317.6 Å) and P212121 (a = 77.0, b = 100.3, c = 100.3 Å), respectively.
Selenomethionine-substituted crystals of the Mg2+ transporter MgtE from T. thermophilus diffracted to 3.5 Å resolution and belonged to space group C2221, with unit-cell parameters a = 118.3, b = 134.9, c = 366.2 Å.
The crystallization and preliminary X-ray studies of the aminoglycoside antibiotic-modifying enzyme hygromycin B phosphotransferase from E. coli are reported.
Robo1 is a large transmembrane receptor expressed on the axon growth cone. Activation of Robo1 by Slit proteins results in axon repulsion from the midline. Here, the purification and crystallization conditions of first two Ig domains of Robo1 are reported.
The crystallization and preliminary X-ray analysis of the family 43 glycoside hydrolase arabinoxylan arabinofuranohydrolase from B. subtilis soaked with xylotriose is described in order to gain insight in the way the enzyme binds its substrates.
By heating a highly amyloidogenic mutant of the human plasma protein transthyretin at 328 K for 48 h, diffraction-quality crystals could be reproducibly produced. The procedure precipitated ~40% of the protein, but rendered what remained in solution more homogenous.
Crystals of hemextin A, a three-finger toxin isolated and purified from African Ringhals cobra (H. haemachatus), are orthorhombic, space group P212121, with unit-cell parameters a = 49.27, b = 49.51, c = 57.87 Å, and diffract to 1.5 Å resolution.
The thrombin-like enzyme saxthrombin has been purified from G. saxatilis snake venom. Crystallization conditions were found and a data set was obtained to 1.43 Å.
The crystallization and preliminary crystallographic studies of LipA, a lipase/esterase secreted by X. oryzae pv. oryzae during its infection of rice plants, are reported.
The expression, purification, and crystallisation of the short-chain dehydrogenases WbmF, WbmG and WbmH from B. bronchiseptica are described. Native diffraction data to 1.5, 2.0, and 2.2 Å were obtained for the three proteins, together with complexes with nucleotides.
Native ACTIBIND was successfully crystallized and it was shown that the interaction between ACTIBIND and actin is in a molar ratio of 1:2, with a binding constant of 16.17 × 104 M −1.
Recombinant PRRSV 3CL protease was crystallized and the crystals diffracted to 2.1 Å resolution.