Crystallization and preliminary crystallographic analysis of cytochrome c553 peroxidase from Nitrosomonas europaea.
The di-heme peroxidase (cytochrome c553 peroxidase) from Nitrosomonas europaea has been crystallized in a form suitable for high-resolution X-ray structure determination. A complete data set was obtained to 2.5A and the data were indexed in space group P2(1) with a = 88.79 A, b = 55.93 A, c = 144.37 A, beta = 103.87 degrees. The self-rotation function indicates one homodimer per asymmetric unit.
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Department of Molecular Biology and Biochemistry, University of California at Irvine 92717, USA.
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Sundaramoorthy
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Arciero
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Hooper
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Poulos
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D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D003578:Cytochrome-c Peroxidase / Q000737:chemistry* / Q000302:isolation & purification*; D006418:Heme; D008969:Molecular Sequence Data; D009606:Nitrosomonas / Q000201:enzymology*; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D017386:Sequence Homology, Amino Acid
D006418:Heme; C086955:cytochrome C553 peroxidase; D003578:Cytochrome-c Peroxidase