issue contents

Journal logoBIOLOGICAL
ISSN: 1399-0047

November 2011 issue

Highlighted illustration

Cover illustration: Asymmetric unit of the galactose-binding Sarcocystis muris lectin SML-2 at 1.95 Å resolution (p. 936). Three dimers are shown in front of the 16 Å resolution ab initio structure discussed by Müller et al. (2006, Acta Cryst. D62, 533-540). Secondary structure plot by CHIMERA [Pettersen, et al. (2004) J. Comput. Chem. 25, 1605-1612].

research papers

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The crystal structure of Mason–Pfizer monkey virus protease folded as a monomer has been solved by molecular replacement using a model generated by players of the online game Foldit. The structure shows at high resolution the details of a retroviral protease folded as a monomer which can guide rational design of protease dimerization inhibitors as retroviral drugs.

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A large-scale study indicates a correlation between thermal stability, as measured using a simplified Thermofluor assay, and crystallization likelihood.

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Pyridyl derivatives of vanillin increase the fraction of the more soluble oxygenated sickle hemoglobin and/or directly increase the solubility of deoxygenated sickle hemoglobin. Crystallographic analysis reveals the structural basis of the potent and dual antisickling activity of these derivatives.

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Glucokinase (GK) catalyses the formation of glucose 6-­phosphate from glucose and ATP. Here, the first structures of a GK–glucose complex without activator, of GK–glucose–AMP-PNP and of GK–glucose–AMP-PNP with a bound activator are reported.

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The PAN-modular structure of the parasite Sarcocystis murismicroneme protein SML-­2 and of the complex with 1-thio-β-D-galactose SML-­2 was determined by SAD-sulfur phasing. The crystallographic analysis reveals a dimeric lectin structure and the structural basis of the protein's stability in the intestinal tract of intermediate and final hosts, and suggests a role for SML-2 during host-cell invasion.

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The limitations of weighting between the sum of chemical and data-based targets in macromolecular crystallographic refinement based on comparing the gradients or Hessian diagonal terms of the two potential functions are demonstrated, especially in the context of a maximum-likelihood target that is inherently weighted by the model and data errors

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Possible causes of the instability of crystallographic refinement are discussed and a criterion of model convergence is proposed.

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A challenging case of crystallization of a human nuclear protein complex consisting of two very similar proteins is described. We highlight the considerations to be made in construct design to obtain diffraction-quality crystals of multi-domain, multi-subunit proteins.

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Crystal structures of the human mitochondrial helicase hSuv3 in complex with AMPPNP and with a short strand of RNA are presented.
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