The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes

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.

Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension

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.

High-resolution structures of bacterially expressed soluble human CD59

The X-ray crystallographic structure of the complement regulator CD59 at 1.15 Å resolution hints at modes of interaction with C8/C9.

A structural insight into lead neurotoxicity and calmodulin activation by heavy metals

Crystal structures of human recombinant calmodulin were determined in the presence of lead and barium ions.

Expression, purification, crystallization and preliminary crystallographic analysis of the mouse transcription factor MafB in complex with its DNA-recognition motif Cmare

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.

Purification, crystallization and preliminary crystallographic characterization of the α2,6-sialyltransferase from Photobacterium sp. JT-ISH-224

Crystallization of the α2,6-sialyltransferase from Photobacterium.

Crystallization and preliminary X-ray analysis of a decameric form of cytosolic thioredoxin peroxidase 1 (Tsa1), C47S mutant, from Saccharomyces cerevisiae

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.

Crystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein family

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.

Crystallization and preliminary X-ray diffraction analysis of a soluble domain of the putative zinc transporter CzrB from Thermus thermophilus

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.

Crystallization and preliminary X-ray diffraction analysis of the cytosolic domain of the Mg²⁺ transporter MgtE

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.

Crystallization and preliminary X-ray diffraction analysis of the full-length Mg²⁺ transporter MgtE

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.

Crystallization and preliminary crystallographic analysis of hygromycin B phosphotransferase from Escherichia coli

The crystallization and preliminary X-ray studies of the aminoglycoside antibiotic-modifying enzyme hygromycin B phosphotransferase from E. coli are reported.

Cloning, expression, crystallization and preliminary X-ray analysis of the first two Ig domains from human Roundabout 1 (Robo1)

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.

Crystallization and preliminary X-ray analysis of an arabinoxylan arabino­furano­hydrolase from Bacillus subtilis

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.

Heating of proteins as a means of improving crystallization: a successful case study on a highly amyloidogenic triple mutant of human transthyretin

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.

Crystallization and preliminary X-ray diffraction analysis of hemextin A: a unique anticoagulant protein from Hemachatus haemachatus venom

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.

Purification, crystallization and preliminary X-ray diffraction analysis of saxthrombin, a thrombin-like enzyme from Gloydius saxatilis venom

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.

Crystallization and preliminary crystallographic studies of LipA, a secretory lipase/esterase from Xanthomonas oryzae pv. oryzae

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.

Cloning, expression, purification and preliminary crystallographic analysis of the short-chain de­hydrogenase enzymes WbmF, WbmG and WbmH from Bordetella bronchiseptica

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.

Binding assay and preliminary X-ray crystallographic analysis of ACTIBIND, a protein with anticarcinogenic and antiangiogenic activities

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.

Molecular cloning, expression, purification and crystallographic analysis of PRRSV 3CL protease

Recombinant PRRSV 3CL protease was crystallized and the crystals diffracted to 2.1 Å resolution.