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  • Title: Preliminary investigation of crystals of lipase I from Rhizopus niveus.
    Author: Kohno M, Kugimiya W, Hashimoto Y, Morita Y.
    Journal: J Mol Biol; 1993 Feb 05; 229(3):785-6. PubMed ID: 8433372.
    Abstract:
    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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