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

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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 × 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 ̊. © 1995.

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Rush, C., Willetts, A., Davies, G., Dauter, Z., Watson, H., & Littlechild, J. (1995). Purification, crystallisation and preliminary X-ray analysis of the vanadium-dependent haloperoxidase from Corallina officinalis. FEBS Letters, 359(2–3), 244–246. https://doi.org/10.1016/0014-5793(95)00055-E

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