Preliminary crystallographic studies of dimethylsulfoxide reductase from Rhodobacter capsulatus

被引：8

作者：

Bailey, S

McAlpine, AS

Duke, EMH

Benson, N

McEwan, AG

机构：

[1] CLRC DARESBURY LAB, WARRINGTON WA4 4AD, CHESHIRE, ENGLAND

[2] UNIV E ANGLIA, SCH BIOL SCI, CTR METALLPROT SPECT & BIOL, NORWICH NR4 7TJ, NORFOLK, ENGLAND

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1996年 / 52卷

关键词：

D O I：

10.1107/S0907444995007712

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Dimethylsulfoxide reductase from the photosynthetic bacterium Rhodobacter capsulatus has been crystallized in two similar forms which are suitable for X-ray structure determination. Both crystals forms belong to space group P4(1)22 or P4(3)22, with cell dimensions a = b = 80.81, c = 229.75 Angstrom (type I crystals) or a = b = 89.30, c = 230.05 Angstrom (type II crystals) and one molecule in the asymmetric unit. Diffraction has been observed to at least 2.0 Angstrom, in type I crystals and to 2.6 Angstrom in type II crystals. Dimethylsulfoxide reductase from Rhodobacter is the simplest molybdenum oxotransferase known and this makes it an ideal model to study the structure and function of this class of enzymes.

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页码：194 / 196

页数：3

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