OVERPRODUCTION, CRYSTALLIZATION, AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE MAJOR COLD SHOCK PROTEIN FROM BACILLUS-SUBTILIS, CSPB

被引:51
作者
SCHINDELIN, H [1 ]
HERRLER, M [1 ]
WILLIMSKY, G [1 ]
MARAHIEL, MA [1 ]
HEINEMANN, U [1 ]
机构
[1] UNIV MARBURG,INST BIOCHEM,W-3550 MARBURG,GERMANY
来源
PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1992年 / 14卷 / 01期
关键词
COLD SHOCK PROTEIN; DNA BINDING; CRYSTALLIZATION; X-RAY DIFFRACTION;
D O I
10.1002/prot.340140113
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
The major cold shock protein from Bacillus subtilis (CspB) was overexpressed using the bacteriophage T7 RNA polymerase/promoter system and purified to apparent homogeneity from recombinant Escherichia coli cells. CspB was crystallized in two different forms using vapor diffusion methods. The first crystal form obtained with ammonium sulfate as precipitant belongs to the trigonal crystal system, space group P3(1)21 (P3(2)21) with unit cell dimensions a = b = 59.1 angstrom and c = 46.4 angstrom. The second crystal form is tetragonal, space group P4(1)2(1)2 (P4(3)2(1)2) with unit cell dimensions a = b = 56.9 angstrom and c = 53.0 angstrom. These crystals grow with polyethylene glycol 4000 as precipitant.
引用
收藏
页码:120 / 124
页数:5
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