issue contents

ISSN: 2053-230X

January 2019 issue

Including invited contributions on state-of-the-art cryo-electron microscopy

Highlighted illustration

Cover illustration: The human peptide hormone endothelin 1 is important as a vasoconstrictor and is thus a key regulator of blood pressure. The structure of endothelin 1in the unbound state has been determined using X-ray diffraction data that were collected in 1992 [McPherson & Larson (2019), Acta Cryst. F75, 47-53]. This structure shows the value of archiving raw data and reporting the experimental details so that methods can be improved and more difficult structures can be determined in the future.


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Two of the Acta Cryst. F editors introduce a number of articles on cryo-electron microscopy.

cryo-electron microscopy

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Transformational advances in transmission electron microscopy at cryogenic temperature (cryo-EM) is enabling atomic-level insight into the three-dimensional structure and therefore the function of biological macromolecules in solution. Contemporary cryo-EM promises to resolve problems in structural biology that were intractable just a few years ago.

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The influence of noise on cross-correlations is revisited. Equations are provided describing the influence of noise on the cross-correlations between single images and averaged images and on those between averaged images.

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To consistently obtain high-resolution cryo-EM structures, the factors influencing single-particle reconstruction need to be understood. Statistics calculated during reconstruction provide a diagnostic tool to assess the amount of data that is required and whether micrograph quality needs to be improved.

scientific commentaries

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An article detailing a structure determination that has been years in the making appears in this months issue of Acta Cryst. F. McPherson and Larson report the structure of the 21-amino acid, human peptide hormone endothelin 1 that was determined using data collected in 1992.

research communications

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The structure of endothelin in the unbound state has been determined using X-ray diffraction data that were collected in 1992. The crystals exhibit higher symmetry than is in fact present, and they are significantly twinned. There is a dimer containing a pseudo-twofold axis in the asymmetric unit.

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The three-dimensional crystal structure of the glutathione reductase from Streptococcus pneumoniae is reported at 2.56 Å resolution.

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The redefined DNA-binding domain (residues 98–239) of human xeroderma pigmentosum complementation group A, a scaffold protein that plays significant roles in DNA-damage verification and recruiting downstream endonucleases to facilitate the repair of DNA lesions in nucleotide-excision repair, was produced and crystallized and its structure was solved.

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NPR4 has been shown to be a key regulator of the salicylic acid-mediated signal perception and transduction pathways. This project aimed to obtain structural details of NPR4, thus elucidating the molecular mechanism of salicylic acid perception and its signalling role in the systemic acquired resistance pathway.
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