issue contents

ISSN: 2053-230X

January 2020 issue

Highlighted illustration

Cover illustration: An oxidized mutant of human mitochondrial branched-chain aminotransferase (hBCAT) [Herbert et al. (2020), Acta Cryst. F76, 14-19]. hBCAT catalyzes the transamination of the branched-chain amino acids leucine, valine and isoleucine and [alpha]-ketoglutarate to their respective [alpha]-keto acids and glutamate. This enzyme thus plays a significant role in amino-acid metabolism and whole-body nitrogen shuttling, in particular with respect to the de novo synthesis of the neurotransmitter glutamate in the brain.

research communications

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This study presents the crystallization and X-ray diffraction analysis of the RING domain of mitochondrial E3 ubiquitin ligase 1 (MUL1-RING) and its complex with Ube2D2.

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The recombinant production and crystallization of the PitA adhesin from the Streptococcus oralis pilus island 2-encoded sortase-dependent pilus is described. Limited proteolysis of PitA and its complex with terbium crystallophore gave greatly improved X-ray diffraction to 2.16 Å resolution and a sufficiently strong anomalous signal for terbium SAD phasing, respectively.

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The crystal structure of the oxidized form of a human mitochondrial branched-chain aminotransferase (hBCATm) mutant was determined. The structural analysis supports the concept that a complex regulation mechanism is involved in hBCATm activity, which depends on the key residue Cys315.

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Eisenia hydrolysis-enhancing protein from Aplysia kurodai, which is of interest as an indispensable protein for aiding the production of glucose from brown algae, has been purified and crystallized. Native and native-SAD X-ray diffraction data were collected at resolutions of 1.20 and 2.48 Å using wavelengths of 1.0 and 2.1 Å, respectively.

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The bacterial transcriptional regulator of cobalt and nickel efflux, RcnR, has been crystallized with an oligonucleotide encompassing its DNA-binding site.

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A purification protocol for the Escherichia coli RnlA–RnlB toxin–antitoxin complex has been established and the complex was crystallized and characterized using SAXS and native mass spectrometry.

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Acinetobacter baumannii undecaprenyl pyrophosphate synthase, a key enzyme in bacterial cell-wall biosynthesis, has been shown via X-ray structures to bind three fragments identified from direct crystal soaking of a cocktailed screening library.
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