issue contents

ISSN: 2053-230X

December 2020 issue

Highlighted illustration

Cover illustration: The hypothetical periplasmic protein PA1624 from the opportunistic pathogen Pseudomonas aeruginosa folds into a unique two-domain structure [Feiler et al. (2020), Acta Cryst. F76, 609-615]. Since PA1624 is only present in this important human pathogen, its unique structure and periplasmic location render it a potential drug target. These results may open new avenues for the discovery and design of antibacterial drugs.

research communications

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SmhA, the A component of the tripartite α-pore-forming toxin from the opportunistic human pathogen Serratia marcescens, has been cloned, overexpressed and purified. Crystals were grown of selenomethionine-derivatized protein, anomalous data were collected, phases were calculated and an initial electron-density map was produced.

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The N-terminal domain of Ssr4 from S. pombe, which is an integral protein in the SWI/SNF and RSC chromatin-remodelling complexes, has been crystallized and its structure has been solved using iodine as a phasing vehicle.

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The structure of barley agmatine coumaroyltransferase, a member of the BAHD acyltransferase superfamily, was elucidated. This is the first report of the structure of an N-acyltransferase from the BAHD superfamily.

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The X-ray crystal structure of benzophenone synthase from G. mangostana L. reveals its active-site cavity and key residues catalyzing the conversion of its preferred substrate benzoyl-CoA to produce 2,4,6-trihydroxybenzophenone as the major product.

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In this study, a structural approach was used to unveil the molecular function of ZC3H41, an essential yet enigmatic protein in the life cycle of T. brucei. Here, the expression, purification and crystallization of this protein are reported.

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Crystal structure analysis of the hypothetical protein PA1624 from P. aeruginosa reveals a novel two-domain protein architecture that is only distantly reminiscent of previously characterized structural domains.


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Cryocrystallography, which is commonly used in macromolecular crystallography, may sometimes reduce the quality of diffraction data and the visibility of crystals owing to frost adhesion. A device has been developed to remove frost by drizzling liquid nitrogen over the crystals, which enabled noise reduction of diffraction images and the centering of crystals with low visibility owing to frost adhesion.

addenda and errata

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