PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE VANADIUM-DEPENDENT HALOPEROXIDASE FROM CORALLINA-OFFICINALIS

Authors
RUSH C WILLETTS A DAVIES G DAUTER Z WATSON H LITTLECHILD J
Citation
C. Rush et al., PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE VANADIUM-DEPENDENT HALOPEROXIDASE FROM CORALLINA-OFFICINALIS, FEBS letters, 359(2-3), 1995, pp. 244-246
Citations number
17
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
359
Issue
2-3
Year of publication
1995
Pages
244 - 246
Database
ISI
SICI code
0014-5793(1995)359:2-3<244:PCAPAO>2.0.ZU;2-U
Abstract
The vanadium-dependent haloperoxidase from the seaweed Corallina offic inalis 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 i s dependent on vanadium for activity. The crystals are grown from poly ethylene glycol (PEG) 6,000 and 0.4 M potassium chloride, They are sta ble and diffract to better than 2 A resolution, They are of a cubic sp ace group I23 (or I2(1)3) with cell dimensions a = b = c = 310 Angstro m.