Crystallography Research Today is a free monthly online journal that collates and summarizes the latest research about Crystallography, including details on x-ray crystals, techniques, analyses, structures.

Crystallization and preliminary crystallographic analysis of beta-L-arabinopyranosidase from Streptomyces avermitilis NBRC14893.

Fujimoto Z, Ichinose H, Harazono K, Honda M, Uzura A, Kaneko S

Protein Research Unit, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan.

Beta-L-arabinopyranosidase from Streptomyces avermitilis NBRC14893 is a monomeric protein consisting of a catalytic domain belonging to glycosyl hydrolase family 27, an unknown domain and a substrate-binding domain belonging to carbohydrate-binding module family 13. The complete enzyme (residues 45-658) has successfully been cloned and homologously expressed in the Streptomyces expression system. beta-L-Arabinopyranosidase was crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to 1.6 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.2, b = 98.9, c = 181.3 A. The Matthews coefficient was calculated to be 2.38 A(3) Da(-1).

Published 29 May 2009 in Acta Crystallogr Sect F Struct Biol Cryst Commun, 65: 632-4.
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Articles on Crystallography published 29 May 2009:

Cloning, overproduction, purification, crystallization and preliminary X-ray diffraction analysis of yeast glutaredoxin Grx5.   Acta Crystallogr Sect F Struct Biol Cryst Commun, 65: 651-3.

Grx5 from the yeast Saccharomyces cerevisiae is a monothiol glutaredoxin that is involved in iron-sulfur cluster biogenesis. Here, yeast Grx5 was cloned and overproduced in Escherichia coli. The purified protein was crystallized using the hanging-drop vapour-diffusion method. Diffraction data for Grx5 were collected to 1.67 A resolution. The crystal of Grx5 belonged to space group R3, with unit-cell parameters a = b = 85.12, c = 48.95 A, alpha = beta = 90.00, gamma = 120.00 degrees . [Abstract] [Full-text]

Crystallization and preliminary crystallographic studies of human RIG-I in complex with double-stranded RNA.   Acta Crystallogr Sect F Struct Biol Cryst Commun, 65: 648-50.

Retinoic acid inducible gene-I (RIG-I) is an essential component of the innate immune system that is responsible for the detection and elimination of invading viruses. RIG-I recognizes viral RNAs inside the cell and then initiates downstream signalling to activate the IRF-3 and NF-kappaB genes, which results in the production of type I interferons. RIG-I is composed of an N-terminal CARD domain for signalling and C-terminal helicase and repressor domains for RNA recognition. A RIG-I-RNA binding ... [Abstract] [Full-text]

Crystallization and preliminary X-ray diffraction analysis of Q4DV70 from Trypanosoma cruzi, a hypothetical protein with a putative thioredoxin domain.   Acta Crystallogr Sect F Struct Biol Cryst Commun, 65: 641-4.

Q4DV70 is annotated in the Trypanosoma cruzi CL Brener genome as a hypothetical protein with a predicted thioredoxin-like fold, although the catalytic cysteine residues that are conserved in typical oxidoreductases are replaced by serine residues. Gene-expression analysis indicates that this protein is differentially expressed during the T. cruzi life cycle, suggesting that it plays an important role during T. cruzi development. The gene coding for Q4DV70 was cloned and the protein was ... [Abstract] [Full-text]

Overexpression, purification, crystallization and preliminary X-ray studies of Vibrio cholerae EpsG.   Acta Crystallogr Sect F Struct Biol Cryst Commun, 65: 629-31.

EpsG is the major pseudopilin protein of the Vibrio cholerae type II secretion system. An expression plasmid that encodes an N-terminally truncated form of EpsG with a C-terminal noncleavable His tag was constructed. Recombinant EpsG was expressed in Escherichia coli; the truncated protein was purified and crystallized by hanging-drop vapor diffusion against a reservoir containing 6 mM zinc sulfate, 60 mM MES pH 6.5, 15% PEG MME 550. The crystals diffracted X-rays to a resolution of 2.26 A and ... [Abstract] [Full-text]

Crystallization and preliminary X-ray studies of the N-domain of the Wilson disease associated protein.   Acta Crystallogr Sect F Struct Biol Cryst Commun, 65: 621-4.

Wilson disease associated protein (ATP7B) is essential for copper transport in human cells. Mutations that affect ATP7B function result in Wilson's disease, a chronic copper toxicosis. Disease-causing mutations within the N-domain of ATP7B (WND) are known to disrupt ATP binding, but a high-resolution X-ray structure of the ATP-binding site has not been reported. The N-domain was modified to delete the disordered loop comprising residues His1115-Asp1138 (WNDDelta(1115-1138)). Unlike the ... [Abstract] [Full-text]

Crystallization and preliminary X-ray analysis of the V domain of human nectin-2.   Acta Crystallogr Sect F Struct Biol Cryst Commun, 65: 615-7.

Nectin-2 belongs to a family of immunoglobulin-like cell adhesion molecules that are characterized by the presence of three immunoglobulin-like domains (V, C2 and C2) in the extracellular region. The V domain plays important roles in cell adhesion, NK cell activation and the entry of some herpesvirus. In this study, the V domain of human nectin-2 was expressed in Escherichia coli in the form of inclusion bodies, which were subsequently denatured and refolded. The soluble protein was ... [Abstract] [Full-text]

Crystallization and X-ray diffraction data collection of topoisomerase IV ParE subunit from Xanthomonas oryzae pv. oryzae.   Acta Crystallogr Sect F Struct Biol Cryst Commun, 65: 612-4.

Topoisomerase IV is involved in topological changes in the bacterial genome using the free energy from ATP hydrolysis. Its functions are the decatenation of daughter chromosomes following replication by DNA relaxation and double-strand DNA breakage. In this study, the N-terminal fragment of the topoisomerase IV ParE subunit from Xanthomonas oryzae pv. oryzae was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.15 A resolution using a ... [Abstract] [Full-text]

Crystallization and preliminary X-ray crystallographic analysis of two dimeric hyperthermostable thioredoxins isolated from Sulfolobus solfataricus.   Acta Crystallogr Sect F Struct Biol Cryst Commun, 65: 604-7.

The thioredoxin system of the archaeon Sulfolobus solfataricus involves a number of different proteins: two thioredoxin reductases (SsTrxRB2 and SsTrxRB3), two distinct thioredoxins (SsTrxA1 and SsTrxA2) and a disulfide oxidoreductase (SsPDO). Here, the crystallization and preliminary crystallographic analyses of SsTrxA1 and SsTrxA2, two dimeric proteins endowed with extraordinary thermal stability, are reported. In addition to the functional thioredoxin domain, both SsTrxA1 and SsTrxA2 present ... [Abstract] [Full-text]

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