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Purification, crystallization and phase determination of the DR1998 haem b catalase from Deinococcus radiodurans
Author(s) -
Borges Patrícia T.,
Miranda Cecília S.,
Santos Sandra P.,
Carita João N.,
Frazão Carlos,
Romão Célia V.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x1400764x
Subject(s) - deinococcus radiodurans , crystallization , catalase , deinococcus , phase (matter) , chemistry , microbiology and biotechnology , biology , biochemistry , enzyme , dna , organic chemistry
The protective mechanisms of Deinococcus radiodurans against primary reactive oxygen species involve nonenzymatic scavengers and a powerful enzymatic antioxidant system including catalases, peroxidases and superoxide dismutases that prevents oxidative damage. Catalase is an enzyme that is responsible for the conversion of H 2 O 2 to O 2 and H 2 O, protecting the organism from the oxidative effect of H 2 O 2 . This study reports the purification and crystallization of the DR1998 catalase from D. radiodurans . The crystals diffracted to 2.6 Å resolution and belonged to space group C 222 1 , with unit‐cell parameters a = 97.33, b = 311.88, c = 145.63 Å, suggesting that they contain four molecules per asymmetric unit. The initial phases were determined by molecular replacement and the obtained solution shows the typical catalase quaternary structure. A preliminary model of the protein structure has been built and refinement is currently in progress.