Crystallization and preliminary X-ray analysis of catalase-peroxidase from the halophilic archaeon Haloarcula marismortui.
Catalase-peroxidases are bifunctional enzymes found in many microorganisms. Crystals of catalase-peroxidase from the halophilic archaeon Haloarcula marismortui were obtained using the hanging-drop vapour-diffusion method. The rhombic plate-shaped crystals were grown from purified protein solution using (NH(4))(2)SO(4) as precipitant at 293 K. The crystal belongs to the monoclinic system, space group C2, and diffracted beyond 2.0 A resolution.
Yamada
Y
Y
Department of Life Science, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
Saijo
S
S
Sato
T
T
Igarashi
N
N
Usui
H
H
Fujiwara
T
T
Tanaka
N
N
D019843:Archaeal Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D019614:Haloarcula marismortui / Q000201:enzymology*; D010544:Peroxidases / Q000737:chemistry*; D011487:Protein Conformation
D019843:Archaeal Proteins; D010544:Peroxidases; C118175:catalase-peroxidase, Haloarcula