issue contents
February 2023 issue
![Highlighted illustration](/f/issues/2023/02/00/graphics/coverill.gif)
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
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.
PDB reference: D-threonine aldolase, 7yqa
The 2 Å resolution crystal structure of rsCherryRev1.4 illustrates dimer formation via a disulfide linkage in a fluorescent protein.
PDB reference: dimeric rsCherryRev1.4, 8bgl
Open
access
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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.
PDB reference: NPC1 luminal domain C, 8eus