Crystallization of Pichia pastoris lysyl oxidase

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 P2₁2₁2₁, with unit-cell parameters a = 163.7, b = 316.1, c = 84.0 Å, diffract to 2.65 Å resolution. Monoclinic crystals belonging to space group C2, with unit-cell parameters a = 248.4, b = 121.1, c = 151.8 Å, β = 124.6°, diffract to 1.65 Å 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.