issue contents

ISSN: 2053-230X

March 2020 issue

Highlighted illustration

Cover illustration: Structural characterization of mitochondrial citrate synthase 4 from Arabidopsis thaliana [Nishio & Mizushima (2020), Acta Cryst. F76, 109-115]. Citrate synthase catalyzes the first reaction in the TCA cycle - a central metabolic pathway that is responsible for the synthesis of several important molecules that provide a major source of cellular energy in plants.

research communications

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The crystal structure of mitochondrial citrate synthase 4 from Arabidopsis thaliana was determined at a resolution of 2.69 Å and is the first structure of a plant mitchondrial citrate synthase.

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The structure of the human TRPV1 ankyrin-repeat domain was determined by X-ray crystallography. This structure showed a unique solvent-accessible pocket near Cys258 and a unique conformation of its finger loop 3, the conformation of which is significantly different from that in the rat homologue.

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The Legionella pneumophila phospholipase named PlaA is a secreted effector that plays an essential role in maintaining the integrity of Legionella-containing vacuoles in L. pneumophila pathogenesis. Crystals of PlaA and its selenomethionine-substituted form were used for X-ray analysis and diffracted to resolutions of 2.2 and 2.7 Å, respectively.

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Crystal structures of Bacillus subtilis BacF provide an insight into stereospecific substrate recruitment in a fold type I transaminase enzyme.

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The structure of neutral invertase 2 from Arabidopsis thaliana was solved at 3.4 Å resolution. This first structure of a GH100 family enzyme from a higher plant reveals a remarkable similarity to that of the neutral invertase InvA from the cyanobacterium Anabaena, pointing to high evolutionary conservation.
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