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Journal logoSTRUCTURAL
ISSN: 2059-7983

January 2023 issue

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Cover illustration: Frataxin is a key protein in the biosynthesis of iron–sulfur clusters in mitochondria. The hereditary cardiodegenerative and neuro­degenerative disease Friedreich's ataxia arises from either an inability to produce sufficient quantities or the production of a nonfunctional form of this protein. Rodrigues et al. [(2023), Acta Cryst. D79, 22–30] have studied frataxin from Drosophila melanogaster using both X-ray crystallography and NMR spectroscopy.

research papers

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The crystal structure of a covalently linked Aurora-A–MYCN complex is reported, enabling drug design and screening studies.

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A new protocol, DAQ-refine, for evaluating a protein model built from a cryo-EM map and applying local structure refinement is described.

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The structure of Drosophila melanogaster frataxin (Dfh) was derived by X-ray crystallography and studied by NMR spectroscopy. The crystal and solution structures are extremely similar. NMR spectroscopy was also used to identify the iron-binding location on helix 1 and strand 1 of Dfh.

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A scoring function has been developed for the prediction of protein complex interfaces based on neighboring amino acids.

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The crystal structures of two permuted halves of a ribose-binding protein from Thermotoga maritima provide insights into the evolution of the periplasmic binding protein fold from a flavodoxin-like precursor by duplication and domain swapping.

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Atomistic simulations enhance protein crystallography, yielding mechanistic insights into a protein kinase involved in the regulation of fundamental biological processes that include metabolism, development, memory and immune response.

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Key physical principles and methods for collecting crystallographic data from biomolecular systems at room temperature and, more generally, at temperatures between ∼200 and ∼350 K are reviewed and discussed.
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