issue contents

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047

December 2005 issue

Highlighted illustration

Cover illustration: Residues Phe118 and Phe119 (gold) at the C terminus of murine angiogenin are cradled in a hydrophobic pocket. Extensive interactions with residues from the pocket base (blue) and collar (red) may underly the relatively low enzymatic activity of the protein (p. 1568).

research papers


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A simple method to increase the stability of drops used in protein crystallization is characterized with respect to drop size and composition. This method may improve crystallization outcomes and simplify crystallization apparatus.

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The X-ray crystal structure of murine angiogenin indicates that the protein is a useful alternative to the human orthologue for the study of angiogenin structure–function relationships and that the crystals may be suitable for inhibitor-binding studies.

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The crystal structure of the complex formed between phospholipase A2 and niflumic acid has been determined at 2.5 Å resolution and refined to an R factor of 0.187. The structure revealed extensive interactions between niflumic acid and the residues of the substrate-binding site.

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The DNA fragment d(AAATATTT) has been crystallized as long columns of stacked duplexes in a helical arrangement. The columns show a pseudohexagonal organization in the crystal, with no direct interactions among them.

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The structure of C. vibrioforme 5-aminolaevulinic acid dehydratase complexed with the irreversible inhibitor 4,7-­dioxosebacic acid has been solved.

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Least-squares refinement of rubrerythrin automatically converted a trans peptide to one with a cis conformation. The structural transition is characterized by small localized atomic shifts involving a non-ideal linear bond angle within the peptide.

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The crystal structure of M. tuberculosis thioredoxin reductase has been determined to 3 Å resolution. Examination of TLS parameters and normal-mode analysis reveal interesting dynamic behaviour of the enzyme. Lack of involvement of the NADPH domain in crystal contacts suggests that this disorder might represent inherent flexibility of the NADPH domain in the structure.

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44 samples of tetragonal hen egg-white lysozyme were obtained as a series of polycrystalline precipitates at 277 K and room temperature in the pH range between 6.56 and 3.33. The precipitates were investigated by the collection of high-resolution powder X-ray diffraction data at 295 K.

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A multivariate likelihood function extends the resolution and phase quality required for successful automated model building with iterative refinement in many test cases.

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The crystal structure of aluminium-bound ovotransferrin has been determined at 2.15 Å resolution. The aluminium-bound form has almost the same overall structure and metal-coordination sites as the iron-bound form.

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An algorithm is proposed to more generally and efficiently correct experimental error in X-­ray crystal diffraction data.

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A new crystal form of ribonucleotide reductase R2 from E. coli has been obtained and the structure of the dimanganese(II) form has been refined to 2.6 Å resolution. The crystallization conditions and structure are compared with previous results.

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The crystal structure of the 28.3 kDa At4g34215 protein was determined at 1.6 Å resolution. The structure reveals a variation of the active site involved in the formation of an oxyanion hole that has not previously been described in the SGNH-hydrolase superfamily of enzymes.

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Macromolecular crystallization data were collated while parsing information from the Protein Data Bank into a relational database. These data are an up-to-date but incomplete record of current crystallization trends.

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The crystal structure of an acidic phospholipase A2 chemically modified with p-bromophenacyl revealed a novel oligomeric conformation. The abolition of pharmacological activities by the ligand may be related to these structural changes.

short communications


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The influence of an external applied potential on the growth of ferritin crystals from horse spleen is described.
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