Isolation, crystallization and preliminary X-ray analysis of a methanol-induced corrinoid protein from Moorella thermoacetica

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Weihong ZhouBi Cheng Wang

Abstract

A corrinoid protein was induced and overexpressed in methanol-grown cells of the thermophilic anaerobic bacterium Moorella thermoacetica. The protein was purified from cytosolic extracts. After screening for crystallization conditions and optimization, crystals were obtained that diffracted strongly on a rotating-anode X-ray source. A diffraction data set was collected and processed including reflections to 1.9 A resolution. Reflections were indexed in a primitive orthorhombic cell with unit-cell parameters a = 55.69, b = 62.74, c = 34.54 A. N-terminal amino-acid sequencing indicates that the crystals contain a C-terminal fragment of the protein.

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Citations

Dec 5, 2006·Proceedings of the National Academy of Sciences of the United States of America·Christoph H HagemeierUlrich Ermler
Jul 7, 2015·Environmental Microbiology·Michael VisserAlfons J M Stams
Jul 31, 2013·Acta Crystallographica. Section D, Biological Crystallography·Hanno SjutsDavid Leys
Nov 30, 2012·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Ronny C HughesJoseph D Ng
Jul 14, 2018·Environmental Microbiology·Florian KrempVolker Müller

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