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

H. Kaljunen, Chiara Gasparetti, Kristiina Kruus, J. Rouvinen, Nina Hakulinen

Research output: Contribution to journalArticleScientificpeer-review

6 Citations (Scopus)

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 languageEnglish
Pages (from-to)672-674
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number6
DOIs
Publication statusPublished - 2011
MoE publication typeA1 Journal article-refereed

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Aspergillus oryzae
Catechol Oxidase
Aspergillus
oxidase
X ray analysis
Crystallization
enzymes
X-Rays
crystallization
Copper
Fungi
Enzymes
copper
Quinones
Crystals
x rays
fungi
quinones
cells
purification

Cite this

@article{66b3d69b0ba642e38a3e5794b0bdf1ce,
title = "Crystallization and preliminary X-ray analysis of Aspergillus oryzae catechol oxidase",
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 {\AA} resolution and belonged to space group P3221, with unit-cell parameters a = b = 118.9, c = 84.5 {\AA}, = = 90, = 120°. A preparation containing only the shorter form (39.3 kDa) produced crystals that diffracted to 2.9 {\AA} resolution and belonged to space group P212121, with unit-cell parameters a = 51.8, b = 95.3, c = 139.5 {\AA}, = = = 90°.",
author = "H. Kaljunen and Chiara Gasparetti and Kristiina Kruus and J. Rouvinen and Nina Hakulinen",
year = "2011",
doi = "10.1107/S1744309111010141",
language = "English",
volume = "67",
pages = "672--674",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "International Union of Crystallography",
number = "6",

}

Crystallization and preliminary X-ray analysis of Aspergillus oryzae catechol oxidase. / Kaljunen, H.; Gasparetti, Chiara; Kruus, Kristiina; Rouvinen, J.; Hakulinen, Nina.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 67, No. 6, 2011, p. 672-674.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Crystallization and preliminary X-ray analysis of Aspergillus oryzae catechol oxidase

AU - Kaljunen, H.

AU - Gasparetti, Chiara

AU - Kruus, Kristiina

AU - Rouvinen, J.

AU - Hakulinen, Nina

PY - 2011

Y1 - 2011

N2 - 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°.

AB - 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°.

U2 - 10.1107/S1744309111010141

DO - 10.1107/S1744309111010141

M3 - Article

VL - 67

SP - 672

EP - 674

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - 6

ER -