issue contents

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047

August 2008 issue

Highlighted illustration

Cover illustration: Examples of recently remediated PDB entries with regular noncrystallographic symmetry (p. 874). Top left: yellow mottle virus (1f2n); top right: rhinovirus (4rhv); bottom left: pneumolysin (2bk1); center right: tobacco mosaic virus coat protein aggregate (1ei7); bottom right: cucumber green mottle mosaic virus (1cgm).

research papers


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Crystal structures of urate oxidase from A. globiformis and of its complexes with uric acid, allantoate and 8-azaxanthin demonstrate details of substrate recognition and catalysis.

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Improved classification of images from crystallization experiments is obtained using multiple classifiers to combine different feature-extraction methods.

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A pattern-recognition-based method for the identification of planar objects in crystallographic electron-density maps is presented. The accuracy of the located centres of the planes is of the order of 0.5 Å.

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The structure of the 1918 H1N1 neuraminidase was determined to 1.65 Å from crystals with a lattice-translocation defect using uncorrected, as well as corrected, diffraction data.

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The short hydrogen bonds in rhamnogalacturonan acetylesterase have been investigated by structure determination of an active-site mutant, 1H NMR spectra and computational methods. Comparisons are made to database statistics. A very short carboxylic acid carboxylate hydrogen bond, buried in the protein, could explain the low-field (18 p.p.m.) 1H NMR signal.

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A novel phasing method that uses the charge-flipping algorithm has been used to solve the ab initio structure of biological macromolecules at atomic resolution and to determine heavy-atom or anomalous scattering substructures.

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A new data model for PDB entries of viruses and other biological assemblies with regular noncrystallographic symmetry is described.

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Structures of grape dihydroflavonol 4-reductase in complex with NADP+ and various flavonols suggest possible inhibition of the enzyme by flavonols. Initial kinetics experiments confirmed the inhibition and showed its competitive character.

short communications


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Two crystal structures of rhodopsin that were originally described using trigonal symmetry can be interpreted in a hexagonal unit cell with a smaller asymmetric unit.

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The crystal-packing and cohesive energies in the structures of two polymorphs of the title tetrapeptide have been analyzed using molecule–molecule energies calculated using the PIXEL method.
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