Title: Preliminary investigation of crystals of lipase I from Rhizopus niveus Kohno M, Kugimiya W, Hashimoto Y, Morita Y Ref: Journal of Molecular Biology, 229:785, 1993 : PubMed
Lipase I from Rhizopus niveus consists of two polypeptide chains bound non-covalently. Lipase I has been crystallized in a form suitable for X-ray diffraction analysis using the hanging drop method of vapour diffusion at 20 degrees C. The crystals grew at pH 6.0 to 7.0 using 14 to 16% polyethylene glycol 8000 as the precipitant. The crystals are tetragonal with space group P4(1) (or P4(3)) and cell dimensions of a = b = 83.7 A, c = 137.9 A. There are two protein molecules in the asymmetric unit. The diffraction pattern extends to at least 2.5 A resolution.
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Kohno M, Kugimiya W, Hashimoto Y, Morita Y (1993) Preliminary investigation of crystals of lipase I from Rhizopus niveus Journal of Molecular Biology229: 785-6
Kohno M, Kugimiya W, Hashimoto Y, Morita Y (1993) Journal of Molecular Biology229: 785-6
