issue contents

ISSN: 2053-230X

July 2022 issue

Highlighted illustration

Cover illustration: The catalytic domain of human RPTPH [Kim & Ryu (2022), Acta Cryst. F78, 265–269]. Receptor-type protein tyrosine phosphatases (RPTPs) regulate cell growth, differentiation and death via specific signals, and have been implicated in cancer, diabetes and neurological diseases. RPTPH, a member of the type 3 RPTP family, is an important regulator of colorectal cancer and hepatic carcinoma. Here the crystal structure of the catalytic domain of RPTPH has been determined at 1.56 Å resolution.

research communications

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This study reports the unintended crystallization and the structure determination of holo acyl-carrier protein synthase from Mycobacterium smegmatis.

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The crystal structure of the catalytic domain of human RPTPH reveals information for the development of specific inhibitors.

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The crystal structure of the selenomethionine-derivatized halogenase CtcP from Streptomyces aureofaciens, which functions in chlortetracycline biosynthesis, is reported at 2.7 Å resolution. The structure reveals a conserved monooxygenase domain and a unique C-terminal domain. Although FAD was not observed in the structure, the monooxygenase domain has a conserved FAD-binding pocket and active center.

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DotY is a component of the inner membrane-embedded coupling complex T4CC that delivers effectors to the type IV secretion system translocation apparatus. DotY is a highly mobile component of this subcomplex. The crystal structure of DotY on its own was determined and its fold and the connectivity of its secondary-structure elements were established.

methods communications

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The effectiveness of clustering in merging data sets from large numbers of crystals in serial crystallography can be improved by combining multiple clustering techniques using unit-cell parameter-based clustering for very incomplete sets and switching to reflection-based clustering once the preliminary merging has increased the completeness.
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