PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE VANADIUM-DEPENDENT HALOPEROXIDASE FROM CORALLINA-OFFICINALIS
PURIFICATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE VANADIUM-DEPENDENT HALOPEROXIDASE FROM CORALLINA-OFFICINALIS
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DOI：
10.1016/0014-5793(95)00055-e
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发表时间：
1995-02-13
期刊：
影响因子：
3.5
通讯作者：
LITTLECHILD, J
中科院分区：
文献类型：
--
作者：
RUSH, C;WILLETTS, A;LITTLECHILD, J
从海藻Corallina officinalis中提取的钒依赖性卤素过氧化物酶已被纯化至均匀性并结晶，该蛋白据报道为12 x 64,000 Da的六聚体，不含血红素，并且依赖于钒的活性。该晶体由聚乙二醇（PEG） 6000和0.4 M氯化钾生长而成，具有稳定性，衍射分辨率优于2 A，属于立方空间群I23（或I2(1)3），晶胞尺寸为A = b = c = 310埃。
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.