与选择性抑制剂CA074复合的组织蛋白酶B的结晶及初步X射线研究。
Crystallization and preliminary X-ray study of the cathepsin B complexed with CA074, a selective inhibitor.
作者信息
Yamamoto A, Kaji T, Tomoo K, Ishida T, Inoue M, Murata M, Kitamura K
机构信息
Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, Japan.
出版信息
J Mol Biol. 1992 Oct 5;227(3):942-4. doi: 10.1016/0022-2836(92)90234-b.
Cathepsin B from bovine spleen has been purified and crystallized as a complex with a specific inhibitor CA074 [N-(L-3-trans-propylcarbamoyloxirane-2-carbonyl)-L- isoleucyl-L-proline], using the hanging-drop method. The complex crystals obtained from 50 mM-citrate buffer (pH 3.5) belong to the tetragonal space group P4(1) (or P4(3)) with a = 73.06 A and c = 141.59 A, and diffract beyond 2.2 A resolution. There are two complex molecules per asymmetric unit giving a packing density of 3.37 A3/Da and indicating a high solvent content of 63.5%.
已使用悬滴法将来自牛脾脏的组织蛋白酶B纯化并结晶为与特异性抑制剂CA074 [N-(L-3-反式-丙基氨基甲酰氧基环氧乙烷-2-羰基)-L-异亮氨酰-L-脯氨酸] 的复合物。从50 mM柠檬酸盐缓冲液（pH 3.5）中获得的复合物晶体属于四方晶系空间群P4(1)（或P4(3)），a = 73.06 Å，c = 141.59 Å，并且衍射分辨率超过2.2 Å。每个不对称单元有两个复合物分子，堆积密度为3.37 Å3/Da，表明溶剂含量高达63.5%。
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