Schindelin H, Herrler M, Willimsky G, Marahiel M A, Heinemann U
Institut für Kristallographie, Freie Universität Berlin, Federal Republic of Germany.
Proteins. 1992 Sep;14(1):120-4. doi: 10.1002/prot.340140113.
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 A and c = 46.4 A. 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 A and c = 53.0 A. These crystals grow with polyethylene glycol 4000 as precipitant.
使用噬菌体T7 RNA聚合酶/启动子系统对枯草芽孢杆菌的主要冷休克蛋白（CspB）进行了过表达，并从重组大肠杆菌细胞中纯化至表观均一性。采用气相扩散法将CspB结晶为两种不同形式。以硫酸铵作为沉淀剂获得的第一种晶体形式属于三方晶系，空间群为P3(1)21（P3(2)21），晶胞参数a = b = 59.1 Å，c = 46.4 Å。第二种晶体形式为四方晶系，空间群为P4(1)2(1)2（P4(3)2(1)2），晶胞参数a = b = 56.9 Å，c = 53.0 Å。这些晶体以聚乙二醇4000作为沉淀剂生长。
