CRYSTALLIZATION, ACTIVITY ASSAY AND PRELIMINARY-X-RAY DIFFRACTION ANALYSIS OF THE UNCLEAVED FORM OF THE SERPIN ANTICHYMOTRYPSIN

被引:7
作者
WEI, AZ
RUBIN, H
COOPERMAN, BS
SCHECHTER, N
CHRISTIANSON, DW
机构
[1] UNIV PENN,DEPT CHEM,PHILADELPHIA,PA 19104
[2] UNIV PENN,DEPT MED,PHILADELPHIA,PA 19104
[3] UNIV PENN,DEPT DERMATOL,PHILADELPHIA,PA 19104
关键词
PROTEIN CRYSTALLOGRAPHY; PROTEASE INHIBITOR; PROTEIN PROTEIN INTERACTION; BETA-SHEET REARRANGEMENT;
D O I
10.1016/0022-2836(92)90140-F
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Crystals of recombinant wild-type antichymotrypsin have been prepared by the method of vapor diffusion with polyethylene glycol 4000 as a precipitant at pH 5.7. Two crystal forms are observed. One form belongs to tetragonal space group P43212 (or P41212) and has unit cell dimensions a = b = 126 A ̊, c = 243 A ̊, with two molecules in the asymmetric unit. The other crystal form belongs to orthorhombic space group P212121 and has unit cell parameters of a = 73 A ̊, b = 78 A ̊ and c = 80 A ̊, with one molecule in the asymmetric unit. Diffraction intensity measurements have been made on the tetragonal crystal form to a limiting resolution of 4.1 Å, and reflections have been observed on X-ray still photographs to a limiting resolution of 2.5 Å for the orthorhombic form. An activity assay of redissolved tetragonal form crystals indicates that the uncleaved, functional serpin has been crystallized. © 1992.
引用
收藏
页码:273 / 276
页数:4
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