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

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...

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Bibliographic Details
Published in:FEBS letters 1995-02, Vol.359 (2), p.244-246
Main Authors: Rush, Cliff, Willetts, Andrew, Davies, Gideon, Dauter, Zbigniew, Watson, Herman, Littlechild, Jennifer
Format: Article
Language:English
Subjects:
Biotransformation
Corallina officinalis
Crystal
Crystallization
Crystallography, X-Ray
Haloperoxidase
Marine
Peroxidases - chemistry
Peroxidases - isolation & purification
Peroxidases - metabolism
Rhodophyta - enzymology
Seaweed - enzymology
Vanadium - metabolism
Vanadium enzyme
X-ray diffraction
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Summary: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 a = b = c = 310 A ̊ .
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00055-E