issue contents

ISSN: 2053-230X

June 2022 issue

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Cover illustration: An extracellular superoxide dismutase from Onchocerca volvulus [Moustafa et al. (2022), Acta Cryst. F78, 232–240]. O. volvulus is responsible for the neglected disease onchocerciasis or `river blindness'. In the present study, the structure of an extracellular Cu/Zn-SOD from O. volvulus was solved at 1.55 Å resolution and the solution structure of the dimeric protein was verified using small-angle X-ray scattering.

research communications

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Structural and thermal stability analyses of Thermus thermophilus cytochrome c-β (TTCP-β) are presented. It is shown that TTCP-β exhibits higher stability than moderately thermophilic homologue from Methylococcus capsulatus, although both proteins have quite similar folding, heme environment, and subunit composition.

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Preliminary XFEL diffraction data for endo-1,4-β-xylanase from Hypocrea virens are presented.

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An extracellular Cu/Zn superoxide dismutase from Onchocerca volvulus, the causative agent of human onchocerciasis, was purified and crystallized and the structure was solved at 1.55 Å resolution. The solution structure of the dimeric protein was verified using small-angle X-ray scattering. Initial docking studies utilizing previously identified superoxide dismutase inhibitors indicate the potential for future drug development targeting structural features outside the active site.

methods communications

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An in situ X-ray diffraction measurement system using a crystallization plate has been constructed at the SPring-8 protein crystallography beamline. Utilizing small-wedge measurements and incorporating a liquid dispenser to prepare protein–ligand complex crystals, this system will make ligand screening possible.
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