Abstract
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 x 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 A resolution, They are of a cubic space group I23 (or I2(1)3) with cell dimensions a = b = c = 310 Angstrom.
Original language | English |
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Pages (from-to) | 244-246 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 359 |
Issue number | 2-3 |
Publication status | Published - 13 Feb 1995 |
Keywords
- HALOPEROXIDASE
- VANADIUM ENZYME
- CRYSTAL
- X-RAY DIFFRACTION
- BIOTRANSFORMATION
- ASCOPHYLLUM-NODOSUM
- REACTION-MECHANISM
- BROMOPEROXIDASE
- CHLOROPEROXIDASE
- PILULIFERA
- PEROXIDASE
- ENZYME