issue contents

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047

June 2000 issue

Highlighted illustration

Cover illustration: Superposition of chains A, B and C showing the divergence of the C-terminal tail regions within the chorismate mutase trimer (p. 673).

research papers


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The orthorhombic crystal structure of chorismate mutase from B. subtilis has been determined at 1.30 Å.

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The orientation of two lobes in buffalo lactoferrin at 277 K differs considerably from that observed at 303 K but the relative orientations of domains in both lobes at two temperatures are identical. The opening of the iron-binding cleft at the exterior in the N-lobe in buffalo lactoferrin has been found to be the largest among lactoferrins from different species.

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The X-ray structure of azurin II from A. xylosoxidans is reported in the oxidized and reduced forms at 1.75 Å resolution. The one-electron reduction causes very small changes at the Cu site which cannot be defined with confidence at the current resolution.


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The crystal structure of the 20 amino-acid peptide antibiotic mersacidin has been determined by ab initio phasing methods based on data from a merohedrally twinned crystal containing six independent peptide molecules in the asymmetric unit.

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A difference distance matrix algorithm is presented that enables an objective comparison of related protein structures taking into account the experimental uncertainties.

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TEXTAL, an automated system for building protein structures from electron-density maps, is described. This uses pattern recognition to select regions in a database of previously determined structure that are similar in a map of unknown structure. This system represents an approach to protein structure determination and has the potential to reduce the time required to interpret electron-density maps.

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Image-seeking functions have proved to be useful tools in macromolecular crystallography. The application of these functions in the molecular-replacement method has been studied.

crystallization papers


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The fatty-acid biosynthesis protein β-ketoacyl-ACP synthase III has been crystallized from E. coli in two crystal forms and crystallographic data obtained. Both forms diffract to better than 2.0 Å; a dry flash-cooling technique was used to collect the data.

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The crystallization and preliminary X-ray analysis of high-alkaline pectate lyase from Bacillus sp. have been performed. Native data have been collected to 1.5 Å using synchrotron X-rays.

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Crystals of a complex between granulocyte colony-stimulating factor and its soluble receptor have been prepared by the vapour-diffusion method. Two different crystal forms in space groups P41212 and I4122 have been produced using different crystallization conditions.

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Orthorhombic crystals of DsrD protein from a sulfate-reducing bacterium have been obtained. A gold-derivative crystal has been successfully prepared.

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The C-terminal His-tagged E. coli thioesterase I has been expressed, purified and crystallized. The crystals belong to tetragonal space group P41212 or P43212, with unit-cell parameters a = b = 50.85 (7), c = 171.5 (1) Å and diffract to beyond 2.4 Å resolution.

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The Ebola virus matrix protein VP40 has been expressed, purified and crystallized in space group C2. Crystals diffract to 1.9 Å using synchrotron radiation.

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The enzyme phosphomannomutase/phosphoglucomutase from the pathogenic bacterium P. aeruginosa has been crystallized. X-ray diffraction data have been collected on a synchrotron source to 1.75 Å

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Expression, purification, crystallization and a preliminary X-ray diffraction study of Gcy1p, an aldo–keto reductase from S. cerevisiae, are described. Kinetic studies indicate that Gcy1p is indeed an enzyme possessing NADPH-dependent reductase activity.

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A His-tagged form of the ι-carrageenase from A. fortis has been overproduced and crystallized allowing its X-ray structure determination.

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The C-terminal sterile α-motif (SAM) domain of human p73α has been crystallized. Diffraction data to 2.54 Å was collected and the crystal parameters determined (P41212, a = b = 32.02, c = 133.84 Å). A molecular-replacement solution was obtained using the NMR structure of the same protein as a search model.

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Grancalcin, specifically associated with cells originating in the bone marrow, is a cytosolic Ca2+-binding protein, which binds reversibly to secretory vesicles and plasma membranes in the presence of physiological concentrations of Ca2+. Recombinant human grancalcin has been crystallized in the presence and absence of Ca2+.

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Dihydrofolate reductase from bacteriophage T4 has been crystallized in the presence of the cofactor and an inhibitor. Native data have been collected to 1.9 Å resolution using synchrotron X-rays.

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Orthorhombic crystals of Ygr203p, an arsenate reductase homologue from S. cerevisiae, have been obtained. Native data have been collected to 1.9 Å resolution using Cu Kα X-rays.

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Crystals of five different membrane proteins were obtained from a lipidic cubic phase matrix, thus demonstrating the general applicability of this in cubo crystallization method.

short communications


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This paper demonstrates that the anomalous signal from selenomethionine-substituted proteins (as used in MAD) can be significantly enhanced by oxidation.
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