issue contents

Journal logoBIOLOGICAL
ISSN: 1399-0047

March 2008 issue

Highlighted illustration

Cover illustration: The multiple-conformer model of Tyr33 with the maximum-entropy method (MEM) charge density. The MEM charge density is shown as a grey mesh. The difference MEM charge density is shown as a red mesh. The charge-density levels are 0.70 e Å-3 for the MEM map and 0.40 e Å-3 for the difference map (p. 237).

research papers

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The structure of P. citrinum α-1,2-mannosidase has been determined at 1.95 Å resolution in complex with methyl-α-D-lyxopyranosyl-(1′,2)-α-D-mannopyranoside.

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An accurate structural refinement using the maximum-entropy method (MEM) is reported. The reliability factor Rfree in the SHELX refinement was reduced from 18% to 10% by model building based on MEM charge densities.

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L-Asparaginase from Er. carotovora belongs to the family of bacterial amidohydrolases and catalyzes the conversion of L-asparagine to aspartic acid and ammonia and, to a lesser extent, the formation of L-glutamic acid from L-glutamine. The highly homologous L-asparaginases from E. coli and Er. chrysanthemi are widely used as effective anti-leukaemia drugs. Like the majority of L-asparaginases, ErcA also reveals antitumour activity, but differs from EcA and ErchA in antigenic specificity. Therefore, ErcA is of special interest as a potential therapeutic agent and as an enzyme suitable for drug development.

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A study of the specificities of divalent metal cation-binding sites in proteins with known three-dimensional structure is presented.

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Radiation-damage-induced phasing of PdII-bound and CuII-bound complexes of an 18-residue peptide with two disulfide bonds derived from the neurotoxin apamin rested on the differential susceptibility of radiation-sensitive groups in non-isomorphous lattices.

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The crystal structure of human monocyte chemoattractant protein 4 (MCP-4), a member of the CC chemokine family, has been determined at 1.70 Å resolution.

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The first crystal structure of human argininosuccinate synthetase is presented and is compared with its bacterial counterparts.

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The glycerol concentrations necessary to vitrify 1536 high-throughput crystallization-screening cocktails have been determined in order to aid rational prioritization of crystallization leads observed in these cocktails. The concentrations were made by dilution rather than by the replacement of water with glycerol. They therefore serve as a worst-case scenario.

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Several crystal forms of E. coli asparaginase/isoaspartyl peptidase (EcAIII) can be obtained under essentially the same crystallization conditions. They all have P212121 symmetry with similar unit-cell parameters, but show non-isomorphous crystal packing.

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The structure of a second form of aspartate semialdehyde dehydrogenase from V. cholerae has been determined from crystals grow through optimization of the starting buffer conditions. The similarities and differences between isoforms are discussed from both a structural and a functional perspective.

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