CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE DI-HEME CYTOCHROME-C PEROXIDASE FROM PSEUDOMONAS-AERUGINOSA

被引：8
作者：
FULOP, V
LITTLE, R
THOMPSON, A
GREENWOOD, C
HAJDU, J
机构：
[1] UNIV OXFORD,OXFORD CTR MOLEC SCI,OXFORD OX1 3QU,ENGLAND
[2] UNIV E ANGLIA,SCH BIOL SCI,NORWICH NR4 7TJ,NORFOLK,ENGLAND
来源：
JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 232卷 / 04期
关键词：
CYTOCHROME-C551; PEROXIDASE; PERIPLASMIC PROTEIN; CRYSTALLIZATION; X-RAY DIFFRACTION; GLYCOSYLATION;
D O I：
10.1006/jmbi.1993.1472
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Cytochrome c551 peroxidase is a periplasmic enzyme expressed in Pseudomonas 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 P3121 or P3221 with unit cell dimensions of a = b = 113.8 Å, c = 72.0 Å. They are suitable for X-ray analysis and diffract to dmin = 2.5 Å. There is one peroxidase molecule in the crystallographic asymmetric unit. © 1993 Academic Press Limited.
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页码：1208 / 1210
页数：3
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