Crystallization and Preliminary X-ray Analysis of the Di-Haem Cytochrome c Peroxidase from Pseudomonas aeruginosa

Cytochrome c 551 peroxidase is a periplasmic enzyme expressed in Pseudomas aeruginosa at low oxygen tensions. The glycosylated enzyme has been purified to homogeneity and crystallized by vapour diffusion techniques using polyethylene glycol 2000 as the precipitant in the presence of isopropanol. The...

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Veröffentlicht in:	Journal of molecular biology 1993-08, Vol.232 (4), p.1208-1210
Hauptverfasser:	Fülöp, Vilmos, Little, Richard, Thompson, Adrian, Greenwood, Colin, Hajdu, Janos
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Crystalline structure crystallization cytochrome c551 peroxidase Cytochrome-c Peroxidase - chemistry Fundamental and applied biological sciences. Psychology Glycoproteins - chemistry glycosylation Hemeproteins - chemistry Molecular biophysics periplasmic protein Pseudomonas aeruginosa Pseudomonas aeruginosa - enzymology Structure in molecular biology X-Ray Diffraction
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Beschreibung
Zusammenfassung:	Cytochrome c 551 peroxidase is a periplasmic enzyme expressed in Pseudomas aeruginosa at low oxygen tensions. The glycosylated enzyme has been purified to homogeneity and crystallized by vapour diffusion techniques using polyethylene glycol 2000 as the precipitant in the presence of isopropanol. The crystals belong to the trigonal space group P 3 121 or P3 221 with unit cell dimensions of a = b = 113·8 Å, c = 72·0 Å. They are suitable for X-ray analysis and diffract to d min = 2·5 Å. There is one peroxidase molecule in the crystallographic asymmetric unit.
ISSN:	0022-2836 1089-8638
DOI:	10.1006/jmbi.1993.1472