issue contents

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047

May 2007 issue

Highlighted illustration

Cover illustration: The variation among 20 rebuilt versions of the structure of 1cqp [Kallen et al. (1999), J. Mol. Biol. 292, 1-9], obtained by automated iterative model-building, density modification and refinement (see p. 597), set a lower bound on the uncertainty in the coordinates of atoms in any one of the rebuilt models.

research papers


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A comparison of the binding site of mexicain for E-64 with those of other E-64–cysteine protease complexes shows that highly conserved interactions are replaced by other interactions in which water molecules play an essential role.

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Human hair was identified to be a versatile nucleant surface and was applied successfully for the crystallization of various proteins. Despite the rather complex mechanism of heterogeneous crystallization, it was discovered that the surface properties and the chemical composition together define the nucleation properties of the selected surface.


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Arteriviruses form a family of enveloped, positive-sense RNA viruses that includes important agricultural pathogens such as EAV. The EAV nucleocapsid protein forms an arrangement of dimers in the crystal structure that may reflect its organization in the virus.


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Heterogeneity in ensembles generated by independent model rebuilding principally reflects the limitations of the data and of the model-building process rather than the diversity of structures in the crystal.

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An evaluation of the geometrical restraints used in the refinement of protein structures is presented based on currently available protein and small-molecule structural databases.

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The human formylglycine-generating enzyme was cocrystallized with bromide and iodide ions, which, among other positions, occupy an oxygen-binding pocket that is crucial for enzyme catalysis. Halide ions may substitute for xenon in the detection of oxygen-binding sites.

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The crystal structure of a Rac1–GDP–Zn complex shows that Rac1 can coordinate zinc in a tetrahedral fashion by using residues in its biologically relevant switch I and switch II structural regions. Additionally, zinc can replace the normally coordinated magnesium without the perturbation of GDP from the small GTPase.

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A systematic study of the effect of substituting five different residues for large, solvent-exposed and flexible amino acids has been conducted using traditional and alternate reservoir screens. The results suggest a strategy that may enhance the success rates of preparation of X-ray quality crystals of proteins that are otherwise recalcitrant to crystallization in their wild-type form.

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The crystallographic structure of the N114A mutant of the SH3 domain of the Abelson leukaemia virus tyrosine kinase complexed with a high-affinity peptide is reported. An X-ray diffraction data set was collected directly from crystals from the initial screening using the capillary counter-diffusion technique.

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It is shown that a high-pressure cryocooling method enables the phasing of macromolecular structures using either Xe or native S atoms. The method may even be used for crystals in capillaries.

essays


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The origins of molecular and structural biology are briefly discussed in the context of the current status of the field. The future of structure biology is reviewed suggesting that in order to reach a new level of understanding of biological processes is necessary to include the notions of dissipative structures within the conceptual framework of non-equilibrium thermodynamics.
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