issue contents

ISSN: 2053-230X

March 2024 issue

Highlighted illustration

Cover illustration: X-ray structure of the GDP-bound state of GTPase FlhF, a signal recognition particle-type enzyme [Dornes et al. (2024), Acta Cryst. F80, 53–58]. SRP GTPase FlhF is pivotal for spatial-numerical control and bacterial flagella assembly across diverse species, including pathogens.


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The current situation of scientific manuscript peer review is discussed, both generally and as applied to Acta Crystallographica F – Biological Research Communications.

research communications

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This study presents the X-ray structure of FlhF in its GDP-bound state at a resolution of 2.28 Å, exhibiting the classical N- and G-domain fold. Comparative analysis with GTP-loaded FlhF elucidates the conformational changes associated with GTP hydrolysis.

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A heterologous holophytochrome overproduction system has been developed to produce large quantities of three holoprotein constructs of phytochrome B from S. bicolor for crystallization. The results showed that the diffraction quality of the crystals could be improved by removing flexible regions, shifting the fusion tag and changing the type of ligand.

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The NYN domain of human KHNYN was crystallized with a single-stranded RNA and the crystal diffracted to 1.72 Å resolution. The RNase activity of the NYN domain was also demonstrated using different RNAs, together with the binding between the NYN domain of KHNYN and the zinc-finger domain of ZAP.
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