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Crystallization and preliminary X-ray diffraction studies of a corrinoid protein from Sporomusa ovata
U G Wagner1, E Stupperich, P Aulkemeyer
1Institut für Physikalische Chemie, Karl-Franzes-Universität Graz, Austria.
Journal of Molecular Biology
|February 11, 1994
Abstract:
Crystals of a 40 kDa p-cresolyl-cobamide containing protein from Sporomusa ovata have been obtained from polyethyleneglycol solutions at pH 8.5 by the hanging drop technique. The crystals belong to space group C222(1) with cell dimensions a = 110.5(0.2) A, b = 144.0 (0.2) A, c = 110.4 (0.1) A. They diffract to 2.2 A resolution on a rotating anode X-ray source and are suitable for high resolution X-ray diffraction studies.