CRYSTAL QUALITY AND INHIBITOR BINDING BY ASPARTIC PROTEINASES - PREPARATION OF HIGH-QUALITY CRYSTALS OF MOUSE RENIN

被引:5
作者
BADASSO, M [1 ]
SIBANDA, BL [1 ]
COOPER, JB [1 ]
DEALWIS, CG [1 ]
WOOD, SP [1 ]
机构
[1] UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,MOLEC BIOL LAB,MALET ST,LONDON WC1E 7HX,ENGLAND
关键词
D O I
10.1016/0022-0248(92)90274-M
中图分类号
O7 [晶体学];
学科分类号
0702 ; 070205 ; 0703 ; 080501 ;
摘要
Renin from mouse submandibular glands has been highly purified and co-crystallized with a synthetic nonapeptide fragment of rat angiotensinogen in which the scissile Leu-Leu bond has been modified as a hydroxyethylene mimic of the transition state. The strong diffraction from these crystals compared to the native form is discussed in relation to the behaviour of other members of the aspartic proteinase family in crystallisation.
引用
收藏
页码:393 / 399
页数:7
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