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 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 12(1)3) with cell dimensions a = b = c = 310 A.
Rush
C
C
Department of Chemistry, University of Exeter, UK.
Willetts
A
A
Davies
G
G
Dauter
Z
Z
Watson
H
H
Littlechild
J
J
D003460:Crystallization; D018360:Crystallography, X-Ray; D010544:Peroxidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000461:Rhodophyta / Q000201:enzymology*; D012624:Seaweed / Q000201:enzymology*; D014639:Vanadium / Q000378:metabolism*
D014639:Vanadium; D010544:Peroxidases; C026195:bromide peroxidase