Purification, crystallization and preliminary X-ray investigation of quinoprotein methylamine dehydrogenase from Thiobacillus versutu

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Abstract
The enzyme methylamine dehydrogenase or primary-amine:(acceptor) oxidoreductase (deaminating) (EC 1.4.99.3) was purified from the bacterium T. versutus to homogeneity, as judged by polyacrylamide gel electrophoresis. The native enzyme has a Mr of 123,500 and contains four subunits arranged in a .alpha.2.beta.2 configuration, the light and heavy subunits having a Mr of 12,900 and 47,500, respectively. The isoelectric point is 3.9. The purified enzyme was crystallized from 37-42% saturated ammonium sulphate in 0.1 M sodium acetate buffer, pH 5.0. The space group is P321 or P3221, with one .alpha.2.beta.2 molecule in the asymmetric unit. The cell dimensions are: a = b = 13.01 nm; c = 10.40 nm. The X-ray diffraction pattern extends to at least 0.25-nm resolution.