issue contents

ISSN: 2053-230X

September 2022 issue

Highlighted illustration

Cover illustration: The crystal structure of acetylcholine-binding protein from Aplysia californica in complex with the naturally occurring neurotoxin (+)-anatoxin-a [Parker et al. (2022), Acta Cryst. F78, 313–323]. Binding assays and crystallography have been used to try to understand the chemical features and interactions that allow two alkaloid neurotoxins to influence human nicotinic acetylcholine receptors, which are important therapeutic targets.

research communications

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The binding of two potent alkaloid neurotoxins to acetylcholine-binding protein was investigated using calorimetry and fluorescence titration. The crystal structures of two complexes and sequence and structure comparisons inform discussion on the biological implications for interactions with human nicotinic acetylcholine receptor subtypes, which are important therapeutic targets.

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The first structural report of CL-AI from chickpea seeds reveals a trimeric arrangement and structural features that are conserved among 11S globulins.

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Angiogenin is a pathologically relevant but little understood ribonuclease, the interactions of which with RNA are structurally unknown. Here, the first crystal structure of human angiogenin bound to RNA is presented.

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The crystal structure of the hypothetical protein TTHA1873 from T. thermophilus has been determined using X-ray crystallography. At high concentrations, the protein showed visible agglutination of red blood cells; its structural properties and thermal stability are discussed.

addenda and errata

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