issue contents

ISSN: 2053-230X

February 2023 issue

Highlighted illustration

Cover illustration: The reversibly switchable red fluorescent protein rsCherryRev1.4 [Bui et al. (2023), Acta Cryst. F79, 38–44]. In this protein, dimerization has been found to be controlled via disulfide cross-linking, which suggests a possible use in developing redox sensors.

research communications

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The crystal structure of D-threonine aldolase from the green alga Chlamydomonas reinhardtii was determined at 1.85 Å resolution and is the first structure of a eukaryotic D-threonine aldolase to be determined.

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The 2 Å resolution crystal structure of rsCherryRev1.4 illustrates dimer formation via a disulfide linkage in a fluorescent protein.

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New purification protocols for the second luminal domain of Nieman–Pick C1 protein, which serves as the intracellular receptor for Ebola and Marburg viruses, are reported together with a crystal structure, offering a structural view of the Ebola virus binding site.
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