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Purification, crystallisation and preliminary X‐ray analysis of the vanadium‐dependent haloperoxidase from Corallina officinalis
Author(s) -
Rush Cliff,
Willetts Andrew,
Davies Gideon,
Dauter Zbigniew,
Watson Herman,
Littlechild Jennifer
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00055-e
Subject(s) - polyethylene glycol , vanadium , chemistry , potassium , crystallization , random hexamer , nuclear chemistry , crystallography , inorganic chemistry , biochemistry , organic chemistry
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 I 23 (or I2 ,3) with cell dimensions .