Open AccessCrystallization and preliminary X‐ray diffraction analysis of a cold‐adapted catalase from Vibrio salmonicida
Author(s) -
Riise Ellen Kristin,
Lorentzen Marit Sjo,
Helland Ronny,
Willassen Nils Peder
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105041199
Subject(s) - hydrogen peroxide , monoclinic crystal system , catalase , proteus mirabilis , crystallization , mesophile , chemistry , ammonium sulfate , psychrophile , molecule , crystallography , materials science , microbiology and biotechnology , bacteria , biology , escherichia coli , chromatography , biochemistry , organic chemistry , antioxidant , enzyme , genetics , gene
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 P 2 1 , with unit‐cell parameters a = 98.15, b = 217.76, c = 99.28 Å, β = 110.48°. Data were collected to 1.96 Å and a molecular‐replacement solution was found with eight molecules in the asymmetric unit.