Catechol oxidase is an enzyme that catalyzes the oxidation of o-diphenols to the corresponding o-quinones. It is a copper-containing enzyme with a binuclear copper active site. Here, the crystallization and multiple-wavelength anomalous dispersion data collection of catechol oxidase from the mould fungus Aspergillus oryzae are described. During the purification, three forms of the enzyme (39.3, 40.5 and 44.3 kDa) were obtained. A mixture of these three forms was initially crystallized and gave crystals that diffracted to 2.5 Å resolution and belonged to space group P3221, with unit-cell parameters a = b = 118.9, c = 84.5 Å, = = 90, = 120°. A preparation containing only the shorter form (39.3 kDa) produced crystals that diffracted to 2.9 Å resolution and belonged to space group P212121, with unit-cell parameters a = 51.8, b = 95.3, c = 139.5 Å, = = = 90°.
|Number of pages||3|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Publication status||Published - 2011|
|MoE publication type||A1 Journal article-refereed|
Kaljunen, H., Gasparetti, C., Kruus, K., Rouvinen, J., & Hakulinen, N. (2011). Crystallization and preliminary X-ray analysis of Aspergillus oryzae catechol oxidase. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67(6), 672-674. https://doi.org/10.1107/S1744309111010141