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

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1978年 / 122卷 / 01期

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

页码：103 / 107

页数：5

共 13 条

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