X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile.
X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile.
复制标题
交联枯草杆菌嘉士伯在水中与乙腈中的 X 射线晶体结构。
DOI：
10.1006/bbrc.1994.1098
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发表时间：
1994
影响因子：
3.1
通讯作者：
Klibanov,AM
中科院分区：
文献类型：
--
作者：
Fitzpatrick,PA;Ringe,D;Klibanov,AM
通过 X 射线晶体学以 2.3 Å 分辨率在水溶液中解析了与戊二醛轻度交联的枯草杆菌蛋白酶 Carlsberg 的晶体结构。发现它与最近确定的无水乙腈中交联酶的结构几乎相同（Fitzpatrick, P.A., Steinmetz, A.C.U., Ringe, D.A. & Klibanov, A.M. (1993)Proc. Natl. Acad. Sci. USA90, 8653）。后一种结构被发现比水中的刚性明显更高，这可以从它们的平均 B 因子反映出来。两种结构中枯草杆菌蛋白酶结合水分子的数量相似（水和乙腈中分别为 114 和 99），但其中一半结合水的位置不同。
The crystal structure of subtilisin Carlsberg lightly cross-linked with glutaraldehyde was solved in aqueous solution by X-ray crystallography at 2.3 Å resolution. It was found to be virtually identical to the recently determined (Fitzpatrick, P.A., Steinmetz, A.C.U., Ringe, D.A. & Klibanov, A.M. (1993)Proc. Natl. Acad. Sci. USA90, 8653) structure of the cross-linked enzyme in anhydrous acetonitrile. The latter structure was found to be significantly more rigid than in water, as reflected by their average B factors. The numbers of subtilisin-bound water molecules in the two structures are similar (114 and 99 in water and in acetonitrile, respectively), but the locations of some half of these bound waters are distinct.