Crystallization and preliminary crystallographic analysis of cytochrome c553 peroxidase from Nitrosomonas europaea

H Pappa; H Li; M Sundaramoorthy; D Arciero; A Hooper; T L Poulos

doi:10.1006/jsbi.1996.0060

Crystallization and preliminary crystallographic analysis of cytochrome c553 peroxidase from Nitrosomonas europaea

J Struct Biol. 1996 May-Jun;116(3):429-31. doi: 10.1006/jsbi.1996.0060.

Authors

H Pappa¹, H Li, M Sundaramoorthy, D Arciero, A Hooper, T L Poulos

Affiliation

¹ Department of Molecular Biology and Biochemistry, University of California at Irvine 92717, USA.

PMID: 8813001
DOI: 10.1006/jsbi.1996.0060

Abstract

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.

Publication types

Comparative Study
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amino Acid Sequence
Crystallization
Crystallography, X-Ray
Cytochrome-c Peroxidase / chemistry*
Cytochrome-c Peroxidase / isolation & purification*
Heme
Molecular Sequence Data
Nitrosomonas / enzymology*
Pseudomonas aeruginosa / enzymology
Sequence Homology, Amino Acid

Substances

Heme
cytochrome C553 peroxidase
Cytochrome-c Peroxidase