issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

November 2019 issue

Highlighted illustration

Cover illustration: The crystal structure of the P235GK mutant of the arginine-binding protein from Thermotoga maritima in its monomeric state provides clues to the structural determinants of the domain swapping observed in the wild-type protein [Smaldone et al. (2019), Acta Cryst. F75, 707-713]. The data analysis, solution, refinement and validation of this structure were conducted as part of a tutorial session during the Crystallographic Information Fiesta held in Naples, Italy in the summer of 2019 and organized by the Italian Crystallographic Association in partnership with the IUCr.

editorial


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The Editors of Acta Cryst. F describe a new feature that will add an extra dimension to the journal.

methods communications


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An annotation tool is presented that automatically locates amino-acid residues in published papers and matches them to protein structures within the paper. These matches can be provided in context or in a searchable format in order for researchers to better use the existing and future literature.

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An open-source automated microscope capable of capturing both fluorescent and standard images from multi-well protein crystallization plates is described.

research communications




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The crystal structure of the P235GK mutant of the arginine-binding protein from Thermotoga maritima in its monomeric state provides clues to the structural determinants of the domain swapping observed in the wild-type protein.

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The apo-to-holo transition of an enzyme allows insights into the structural hinges that accommodate different ligands within its active site. Here, such a hinge is elucidated in Toxoplasma gondii prolyl-tRNA synthetase and shown in its different possible conformations in two apo forms and two inhibitor-bound forms.
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