Crystallization and preliminary X-ray analysis of catalase-peroxidase fromthe halophilic archaeon Haloarcula marismortui

Authors
Yamada, Y Saijo, S Sato, T Igarashi, N Usui, H Fujiwara, T Tanaka, N
Citation
Y. Yamada et al., Crystallization and preliminary X-ray analysis of catalase-peroxidase fromthe halophilic archaeon Haloarcula marismortui, ACT CRYST D, 57, 2001, pp. 1157-1158
Citations number
14
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
8
Pages
1157 - 1158
Database
ISI
SICI code
0907-4449(200108)57:<1157:CAPXAO>2.0.ZU;2-N
Abstract
Catalase-peroxidases are bifunctional enzymes found in many microorganisms. Crystals of catalase-peroxidase from the halophilic archaeon Haloarcula ma rismortui were obtained using the hanging-drop vapour-diffusion method. The rhombic plate-shaped crystals were grown from purified protein solution us ing (NH4)(2)SO4 as precipitant at 293 K. The crystal belongs to the monocli nic system, space group C2, and diffracted beyond 2.0 Angstrom resolution.