Abstract
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°.
Original language | English |
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Pages (from-to) | 672-674 |
Number of pages | 3 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 67 |
Issue number | 6 |
DOIs | |
Publication status | Published - 2011 |
MoE publication type | A1 Journal article-refereed |