issue contents

ISSN: 2053-230X

April 2020 issue

Highlighted illustration

Cover illustration: Crystal structure of monomeric Amuc_1100 from Akkermansia muciniphila [Mou et al. (2020), Acta Cryst. F76, 168-174]. Many human diseases, such as obesity and diabetes, often involve intestinal microbes. One such probiotic bacterium, Akkermansia muciniphila, has been shown to improve glucose homeostasis and to contribute to gut health. Amuc_1100, an outer membrane in A. muciniphila, may play an important role in the interplay between the microbe and the host.


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Crystallography in its broadest sense has a crucial role to play in addressing the current COVID-19 pandemic. An outpouring of structural information on key viral proteins has resulted and importantly these data have immediately been shared with researchers round the world to speed the discovery of effective therapeutic agents.

research communications

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The crystal structure of human O-phosphoethanolamine phospho-lyase, a pyridoxal 5′-phosphate-dependent enzyme that catalyzes the degradation of O-phosphoethanolamine (PEA) into acetaldehyde, phosphate and ammonia, is reported at 2.05 Å resolution. As PEA is the precursor of phosphatidylethanolamine in the CDP-ethanolamine (Kennedy) pathway, the enzyme is physiologically involved in phospholipid metabolism.

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The crystal structure of monomeric Amuc_1100 (residues 31–317) is reported at 2.1 Å resolution. Structural investigation of Amuc_1100 will shed light on the therapeutic mechanism of Akkermansia muciniphila as well as the formation of its type IV pilus-like structure.

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GlgM is responsible for the biosynthesis of α-maltose-1-phosphate, the building block for the third known biosynthetic pathway to glycogen/α-glucan, which is a target for antimycobacterials. Here, the first known structure of GlgM is reported.

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The crystal structure of the α1 subunit of Arabidopsis thaliana casein kinase 2 was determined in three crystal forms in the absence and presence of the nonhydrolyzable ATP analog AMppNHp.

addenda and errata

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