BamHI核酸内切酶的过表达、纯化及结晶
Overexpression, purification and crystallization of BamHI endonuclease.
作者信息
Jack W E, Greenough L, Dorner L F, Xu S Y, Strzelecka T, Aggarwal A K, Schildkraut I
机构信息
New England Biolabs, Inc., Beverly, MA 01915.
出版信息
Nucleic Acids Res. 1991 Apr 25;19(8):1825-9. doi: 10.1093/nar/19.8.1825.
Abstract
The type II restriction endonuclease BamHI has been expressed in E. coli, producing 100-fold more enzyme than the wild type Bacillus amyloliquefaciens H strain. This high yield has facilitated purification to homogeneity of large amounts of the enzyme, along with its crystallization in a form which diffracts to at least 1.9 A in X-ray analysis.
摘要
II型限制性内切酶BamHI已在大肠杆菌中表达，产生的酶比野生型解淀粉芽孢杆菌H菌株多100倍。这种高产量有助于将大量的酶纯化至同质，同时其结晶形式在X射线分析中衍射至至少1.9埃。
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