issue contents

Journal logoSTRUCTURAL
ISSN: 2059-7983

July 2016 issue

Highlighted illustration

Cover illustration: Neutron and X-ray single-crystal diffraction from protein microcrystals via magnetically oriented microcrystal arrays in gels (Tsukui et al., p. 823). Schematic view of a non-uniform rotating magnetic field applied to a HEWL microcrystal suspension. A HEWL microcrystal suspension was rotated at speeds [omega]slow and [omega]fast (>[omega]slow) in a static magnetic field B. Magnetically oriented microcrystals consolidated in D2O gels may provide a promising means to obtain single-crystal neutron diffraction from proteins that do not crystallize at the sizes required for neutron diffraction structure determination.

research papers

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Single-crystal neutron and X-ray diffraction from lysozyme microcrystals magnetically aligned in gels are reported. Neutron diffraction spots were observed to a resolution of 3.4 Å and the crystal structure was solved at a resolution of 1.76 Å using X-rays at room temperature.

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A two-step process of phase determination in the X-ray structural analysis of the coat protein of a betanodavirus is described. A new indicator, the free fraction, for molecular averaging in real space is introduced to effectively evaluate the phasing power in order to enhance the success of determining new structures.

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Structures of human Gcn5L2 bound to propionyl-CoA and butyryl-CoA show how the active site accommodates different acyl modifications and explain why butyryl-CoA acts as a competitive inhibitor.

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Second harmonic generation correlation spectroscopy was developed as a tool for the characterization of diffusing protein nanocrystals.

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An angular-split/temporal-delay approach offers a solution to crystallographic observations of ultrafast structural dynamics in biological macromolecules.

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The allosteric regulation of S. mutans 2′-deoxycytidylate deaminase by dCTP/dTTP is based on a concentration-dependent competition mechanism. This is the first pair of dTTP/dCTP-bound crystal structures of deoxycytidylate deaminase from the same species to be reported.

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