Open AccessCrystallization and preliminary X‐ray analysis of Aspergillus oryzae catechol oxidase
Author(s) -
Kaljunen Heidi,
Gasparetti Chiara,
Kruus Kristiina,
Rouvinen Juha,
Hakulinen Nina
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111010141
Subject(s) - catechol , aspergillus oryzae , crystallization , enzyme , resolution (logic) , chemistry , oxidase test , catechol oxidase , crystallography , stereochemistry , polyphenol oxidase , biochemistry , organic chemistry , peroxidase , artificial intelligence , computer science
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 P 3 2 21, with unit‐cell parameters a = b = 118.9, c = 84.5 Å, α = β = 90, γ = 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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 51.8, b = 95.3, c = 139.5 Å, α = β = γ = 90°.