issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

March 2008 issue

Highlighted illustration

Cover illustration: Mouse ADP-ribosylhydrolase 3. Ribbon-plot representation and protein solvent-accessible surface representation. The colouring scheme for the protein chain is from the N-terminus (blue) to the C-terminus (red). The solvent-accessible surface is coloured grey and the two Mg2+ ions are shown as cyan spheres (Mueller-Dieckmann, Kernstock,  Mueller-Dieckmann, Weiss & Koch-Nolte, p. 156).

editorial


protein structure communications


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The crystal structure of ADP-ribosylhydrolase 3 from M. musculus has been determined and refined to a resolution of 1.8 Å. A detailed comparison with the human orthologue at the protein-sequence level as well as of the three-dimensional architecture is presented.

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A complex of human carbonic anhydrase II with its inhibitor acetate is described where the ligand is found to bind in an orientation different from that previously described.

crystallization communications


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The enzyme aspartate semialdehyde dehydrogenase from M. tuberculosis has been expressed, purified and crystallized in two different crystal forms.

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The complex between the Ets domain of Ets2 and its target DNA has been crystallized. The crystals diffracted to 3.0 Å resolution.

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The human Brn-5 transcription factor has been crystallized in complex with DNA. Diffraction data were collected to 2.80 Å.

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The peripheral membrane flavoprotein pyruvate oxidase from E. coli has been crystallized in the full-length form and as a proteolytically activated truncation variant lacking the last 23 amino acids at the C-terminus.

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Crystals of A. niger monoamine oxidase variants display P21 or P41212/P43212 symmetry, with eight or two molecules in the asymmetric unit, respectively.

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Ferredoxin-NAD(P)+ reductase from C. tepidum has been overexpressed in E. coli, purified and crystallized. Diffraction data were collected to 2.4 Å resolution.

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A catalytically inactive mutant of the dual-specificity phosphatase H1L from vaccinia virus was expressed recombinantly, purified and crystallized by the microbatch method. The crystals belong to the tetragonal space group P422 and diffraction data were collected to 2.1 Å resolution using a synchrotron-radiation source. Attempts to derivatize these crystals with xenon gas lead to a space-group change to I422 with a smaller unit cell and a diffraction limit of 3.0 Å.

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T. maritima TrmFO was overexpressed, purified and crystallized. A diffraction data set was collected to a resolution of 2.6 Å.

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Crystallization and selenium substructure solution of RsbS from Moorella thermoacetica, the first ab initio phased crystal structure from Diamond.

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Grass carp β2-microglobulin was expressed in E. coli, purified to homogeneity and crystallized using the hanging-drop vapour-diffusion method with PEG 2K as precipitant. The crystals obtained belong to the orthorhombic space group P212121, with unit-cell parameters a = 38.72, b = 40.65, c = 71.12 Å.

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The peptidoglycan N-acetylglucosamine (GlcNAc) deacetylase BC1960 from B. cereus was crystallized in the presence of the substrate (GlcNAc)6. The crystals belonged to space group P41212 and diffracted to 2.38 Å resolution.

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Dihydrodipicolinate synthase (DHDPS), an enzyme in the lysine-biosynthetic pathway, is a promising target for antibiotic development against pathogenic bacteria. Here, the expression, purification, crystallization and preliminary diffraction analysis of DHDPS from C. botulinum are reported.

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A. acidocaldarius Tc-12-31 β-1,4-mannanase was expressed in E. coli and purified. Crystallization and preliminarily X-ray crystallographic studies were performed for both the native mannanase and its selenomethionyl derivative.

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Survival E (SurE) protein from Campylobacter jejuni, a Gram-negative mesophile, has been overexpressed in Escherichia coli as a soluble protein, successfully purified and crystallized in two distinct crystal forms.

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Polyketide synthase-1 from C. sativa has been crystallized. The crystal diffracted to 1.55 Å resolution with sufficient quality for further structure determination.

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A chondroitin sulfate A-binding DBL important in placental malaria has been overproduced, purified and crystallized. Diffraction data were collected to 1.9 Å resolution.

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This study describes the crystallization and preliminary X-ray analysis of the family PL1 polysaccharide lyase RB5312 from the marine bacterium R. baltica. Purified recombinant protein was crystallized; the crystals belonged to space group P212121 and diffracted X-rays to a resolution of 1.8 Å.

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