Crystallization and preliminary X-ray diffraction analysis of the di-haem cytochrome c peroxidase from Pseudomonas stutzeri.
Crystals of cytochrome c peroxidase from Pseudomonas stutzeri were obtained using sodium citrate and PEG 8000 as precipitants. A complete data set was collected to a resolution of 1.6 A under cryogenic conditions using synchrotron radiation at the ESRF. The crystals belong to space group P2(1), with unit-cell parameters a = 69.29, b = 143.31, c = 76.83 A, beta = 100.78 degrees. Four CCP molecules were found in the asymmetric unit, corresponding to a pair of dimers related by local dyads. The crystal packing in the structure shows that the functional dimers can dimerize, as suggested by previous biochemical studies.
Bonifácio
Cecília
C
REQUIMTE, Centro de Química Fina e Biotecnologia, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Monte de Caparica, Portugal.
Cunha
Carlos A
CA
Müller
Axel
A
Timóteo
Cristina G
CG
Dias
João M
JM
Moura
Isabel
I
Romão
Maria João
MJ
D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D003578:Cytochrome-c Peroxidase / Q000737:chemistry*; D019281:Dimerization; D006418:Heme / Q000737:chemistry*; D008958:Models, Molecular; D011549:Pseudomonas / Q000201:enzymology*; D017356:Synchrotrons
D006418:Heme; D003578:Cytochrome-c Peroxidase