issue contents

ISSN: 2053-230X

February 2022 issue

Highlighted illustration

Cover illustration: The urease accessory protein UreF from Klebsiella pneumoniae [Liu et al. (2022), Acta Cryst. F78, 75–80]. Urease is a vital enzyme that is also a virulence factor for K. pneumoniae, an opportunistic pathogen that mostly affects those with weakened immune systems. UreF is an important nickel-binding urease accessory protein involved in the insertion of Ni2+ into the active site of urease.

research communications

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High-resolution apo and cofactor-bound structures of betaine aldehyde dehydrogenase from Burkholderia pseudomallei are described.

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The crystal structure of a short-chain dehydrogenase/reductase from Burkholderia phymatum offers insights into its possible functions and likely inhibitors of its enzymatic functions.

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The 1.35 Å resolution crystal structure of a 15.6 kDa hypothetical protein from the parasite Giardia lamblia was determined as part of structural genomic studies to assign possible functions to hypothetical proteins from infectious agents. The structure has a prototypical endoribonuclease L-PSP (liver perchloric acid-soluble protein) topology with conserved allosteric active-site residues despite lacking any appreciable sequence identity to other members of this superfamily.

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The 1.77 Å resolution crystal structure of the CO-bound state of [NiFe]-hydrogenase from Citrobacter sp. S-77 revealed that the exogenous CO ligand binds to the nickel ion in a bent conformation. The CO-bound state was identified as an EPR-silent Ni-SCO state by EPR and FT-IR spectroscopy.

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The structure of the nickel-binding urease accessory protein UreF from Klebsiella pneumoniae is reported.

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Structures of the ligand-binding domain of human peroxisome proliferator-activated receptor δ in complexes with three novel ligands (JKPL38, JKP39 and JK122) were determined. In addition, the structure of a previously reported complex was updated to higher resolution by obtaining better quality crystals.

methods communications

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A crystal-processing machine that uses a deep-ultraviolet laser has been developed. The machine can improve diffraction data by optimizing the crystal size and shape or by removing unnecessary portions of the crystal.
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