CRYSTALLIZATION AND PRELIMINARY ELECTRON-DIFFRACTION STUDY TO 3.7 A OF DNA HELIX-DESTABILIZING PROTEIN-GP32STARI

被引:25
作者
CHIU, W
HOSODA, J
机构
[1] Donner Laboratory, University of California, Berkeley
关键词
D O I
10.1016/0022-2836(78)90110-9
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
A two-dimensionally large and thin crystal has been obtained from gp32*I, a proteolytically digested product of a DNA helix-destabilizing protein coded by gene 32 in bacteriophage T4. High-resolution electron diffraction patterns (~3.7Å) are recorded from both unstained and stained protein crystals embedded in glucose. The crystal is of orthorhombic space group with a = 62.9 A ̊ and b = 47.3 A ̊. © 1978.
引用
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页码:103 / 107
页数:5
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