Crystallization and preliminary X-ray diffraction analysis of a cold-adapted catalase from Vibrio salmonicida.
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.
Riise
Ellen Kristin
EK
The Norwegian Structural Biology Centre, Faculty of Science, University of Tromsø, N-9037 Tromsø, Norway.
Lorentzen
Marit Sjo
MS
Helland
Ronny
R
Willassen
Nils Peder
NP
D000220:Adaptation, Biological; D044165:Aliivibrio salmonicida / Q000201:enzymology* / Q000502:physiology; D000595:Amino Acid Sequence; D002374:Catalase / Q000737:chemistry* / Q000502:physiology; D002384:Catalysis; D003080:Cold Temperature; D003460:Crystallization; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011513:Proteus mirabilis / Q000201:enzymology; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D011994:Recombinant Proteins; D002374:Catalase