Crystallization and preliminary X-ray diffraction analysis of cytochrome c peroxidase from the purple phototrophic bacterium Rhodobacter capsulatus.
Bacterial cytochrome c peroxidase (BCCP) from Rhodobacter capsulatus was heterologously expressed in Escherichia coli. It was purified to homogeneity and crystallized using the hanging-drop vapour-diffusion method. Diffraction-quality crystals of the enzyme were obtained under two conditions. The first crystal belonged to space group P2(1), with unit-cell parameters a = 99.2, b = 224.7, c = 167.9 A, beta = 105 degrees, and diffracted to 3.5A resolution. The crystallographic asymmetric unit of these crystals contained ten peroxidase molecules. R. capsulatus BCCP also crystallized in space group P2(1)2(1)2(1), with unit-cell parameters a = 67.2, b = 134.4, c = 167.9 A. These crystals diffracted to 2.7 A resolution and contained four peroxidase molecules per crystallographic asymmetric unit.
De Smet
Lina
L
Department of Biochemistry, Physiology and Microbiology, Laboratory for Protein Biochemistry and Protein Engineering, University of Gent, 9000 Gent, Belgium.
Leys
David
D
Van Beeumen
Jozef J
JJ
D002384:Catalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D003578:Cytochrome-c Peroxidase / Q000737:chemistry*; D011487:Protein Conformation; D016354:Rhodobacter capsulatus / Q000737:chemistry / Q000201:enzymology*
D003578:Cytochrome-c Peroxidase