Crystallization and preliminary X-ray analysis of Aspergillus oryzae catechol oxidase

Heidi Kaljunen, Chiara Gasparetti, Kristiina Kruus, Juha Rouvinen, Nina Hakulinen*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

7 Citations (Scopus)


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, = β = 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, = β = = 90°.

Original languageEnglish
Pages (from-to)672-674
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number6
Publication statusPublished - 1 Jun 2011
MoE publication typeA1 Journal article-refereed


  • Aspergillus oryzae
  • catechol oxidases
  • copper oxidases

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