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Crystallization and preliminary X-ray diffraction analysis of a cold-adapted catalase from Vibrio salmonicida.

ABSTRACT: Catalase (EC 1.11.1.6) catalyses the breakdown of hydrogen peroxide to water and molecular oxygen. Recombinant Vibrio salmonicida catalase (VSC) possesses typical cold-adapted features, with higher catalytic efficiency, lower thermal stability and a lower temperature optimum than its mesophilic counterpart from Proteus mirabilis. Crystals of VSC were produced by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 98.15, b = 217.76, c = 99.28 A, beta = 110.48 degrees. Data were collected to 1.96 A and a molecular-replacement solution was found with eight molecules in the asymmetric unit.

SUBMITTER: Riise EK

PROVIDER: S-EPMC2150922 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of a cold-adapted catalase from Vibrio salmonicida.

Riise Ellen Kristin EK Lorentzen Marit Sjo MS Helland Ronny R Willassen Nils Peder NP

Acta crystallographica. Section F, Structural biology and crystallization communications 20051223 Pt 1

Catalase (EC 1.11.1.6) catalyses the breakdown of hydrogen peroxide to water and molecular oxygen. Recombinant Vibrio salmonicida catalase (VSC) possesses typical cold-adapted features, with higher catalytic efficiency, lower thermal stability and a lower temperature optimum than its mesophilic counterpart from Proteus mirabilis. Crystals of VSC were produced by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. The crystals belong to the monoclinic space group P2(1) ...[more]

PMID: 16511268

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