issue contents

ISSN: 2053-230X

April 2017 issue

Highlighted illustration

Cover illustration: An example of a structure solved using cryo-electron microscopy (Vénien-Bryan et al., p. 174).

topical reviews

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Single-particle cryo-electron microscopy (cryo-EM) has gained its `lettres de noblesse' in structural biology. The synergistic convergence of technological and computational advances now make this a feasible method for determining structures at near-atomic to atomic resolution (∼5–2 Å). The potential impact of cryo-EM on drug discovery is discussed, together with how the method can provide information on conformational variability connected to the function of macromolecular complexes.

research communications

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Weak anomalous signals from serendipitously acquired surface-bound Ca atoms/native S atoms from routine data sets, that were not optimized for SAD phasing, were used to successfully phase protein structures.

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The crystal structure of phosphorylated liver kinase B1 peptide in complex with 14-3-3ζ is reported.

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The extracellular adhesion domain of H. pylori adhesin A was crystallized under two conditions using lithium sulfate and ammonium sulfate as the precipitant, which gave rise to two different crystal forms that diffracted to 1.95 and 2.6 Å resolution, respectively.

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The X-ray crystal structure of the RNA-recognition motif of human heterogeneous ribonucleoprotein A18 is reported at 1.77 Å resolution.

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The crystal structure of human Ca2+-bound S100A1 at 2.25 Å resolution is described.

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The structure of XfsHSP17.9, a small heat-shock protein (sHSP) from X. fastidiosa, is similar to those of other sHSPs, having a conserved structural organization. The secondary structure of XfsHSP17.9 is mostly composed of β-strands and a few short α-helices. The XfsHSP17.9 structure reported here reveals a high-order architecture forming a nearly square cavity.

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D. melanogaster enolase was purified and crystallized. It forms a homodimer with an open conformation.

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The growth of crystals of perdeuterated human manganese superoxide dismutase with a unit-cell edge of 240 Å was optimized for neutron data collection. Data were collected to 2.30 Å resolution from a 0.26 mm3 crystal. This is the crystal with the largest unit-cell edge from which data have been collected via neutron diffraction to sufficient resolution where hydrogen positions can be observed.

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The UAM2 protein from O. sativa was cloned, expressed, purified and crystallized, and a complete data set was obtained from the radiation-sensitive crystals by low-dose vector data collection. In addition, it is shown that UAM2 is likely to exist as a monomer in solution and contains at least one intramolecular disulfide bridge or, alternatively, a structural metal ion.
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