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  • Title: Crystallization of Pichia pastoris lysyl oxidase.
    Author: Lee M, Willingham K, Langley D, Maher MJ, Cohen AE, Ellis PJ, Kuchar JA, Dooley DM, Freeman HC, Guss JM.
    Journal: Acta Crystallogr D Biol Crystallogr; 2002 Dec; 58(Pt 12):2177-9. PubMed ID: 12454493.
    Abstract:
    A copper-containing amine oxidase (PPLO) from the yeast Pichia pastoris has been purified and crystallized in two forms. PPLO is a glycoprotein. The molecular mass from SDS-polyacrylamide gels is 112 kDa, consistent with 20% glycosylation by weight (the calculated molecular weight of the polypeptide is 89.7 kDa). Orthorhombic crystals belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 163.7, b = 316.1, c = 84.0 A, diffract to 2.65 A resolution. Monoclinic crystals belonging to space group C2, with unit-cell parameters a = 248.4, b = 121.1, c = 151.8 A, beta = 124.6 degrees, diffract to 1.65 A resolution. Native data have been recorded from each crystal form at 100 K using synchrotron radiation. A self-rotation function for the monoclinic crystal form reveals the presence of a non-crystallographic twofold axis perpendicular to the crystallographic twofold axis, consistent with the presence of two dimers in the asymmetric unit.
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