Purification, crystallisation and preliminary X‐ray analysis of the vanadium‐dependent haloperoxidase from Corallina officinalis

FEBS Letters

Dauter, Zbigniew¹  Littlechild, Jennifer²  Willetts, Andrew²  Davies, Gideon⁴  Watson, Herman³  Rush, Cliff² 

[1] EMBL, c/o DESY, Notkestrasse 85, D-22603, Hamburg, Germany;Departments of Chemistry and Biological Sciences, University of Exeter, Exeter, EX4 4QD, UK;Department of Biochemistry, University of Bristol, Bristol, BS8 1TD, UK;Department of Chemistry, University of York, Heslington, York, YO1 5DD, UK

关键词: Haloperoxidase;    Vanadium enzyme;    Crystal;    X-ray diffraction;    Biotransformation;   

DOI  :  10.1016/0014-5793(95)00055-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The vanadium-dependent haloperoxidase from the seaweed Corallina officinalis has been purified to homogeneity and crystallised. The protein is reported to be a hexamer of 12 × 64,000 Da, contains no haem, and is dependent on vanadium for activity. The crystals are grown from polyethylene glycol (PEG) 6,000 and 0.4 M potassium chloride. They are stable and diffract to better than 2 Å resolution. They are of a cubic space group I23 (or I2,3) with cell dimensions .

【 授权许可】

Unknown