Crystallization and preliminary X-ray study of the cathepsin B complexed with CA074, a selective inhibitor.
Crystallization and preliminary X-ray study of the cathepsin B complexed with CA074, a selective inhibitor.
复制标题
与选择性抑制剂 CA074 复合的组织蛋白酶 B 的结晶和初步 X 射线研究。
DOI:
10.1016/0022-2836(92)90234-b
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发表时间:
1992
影响因子:
5.6
通讯作者:
Kunihiro Kitamura
中科院分区:
文献类型:
--
作者:
Atsushi Yamamoto;Toshio Kaji;K. Tomoo;Toshimasa Ishida;M. Inoue;Mitsuo Murata;Kunihiro Kitamura
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 m m-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 Å resolution. There are two complex molecules per asymmetric unit giving a packing density of 3· 37 Å 3/Da and indicating a high solvent content of 63· 5%.
DOI:
--
发表时间:
1990
期刊:
Biological chemistry Hoppe-Seyler
影响因子:
--
作者:
Sloane,BF;Rozhin,J;Robinson,D;Honn,KV
通讯作者:
Honn,KV