论文部分内容阅读
用分子置换法成功地解得了MBILF-BTRY的晶体结构,并得到了它的立体结构模型。绿豆胰蛋白酶抑制剂属于絲氨酸蛋白酶抑制剂中结构最复杂的Bowman-Birk型抑制剂。这一类型抑制剂的立体结构以前尚未见报道。MBILF-BTRY复合物晶体的晶胞参数为a=62.99,b=63.54,c=69.70,α=β=γ=90°,空间群为P2_12_12_1,复合物分子量约为27500daltons。用理学电机的Ru-300型转靶X光机及AFC-5型四园衍射仪收集了分辨率为3范围内的独立衍射点5142个。以蛋白质数据库所取得的牛胰蛋白酶分子的座标为
The crystal structure of MBILF-BTRY was successfully solved by molecular displacement method, and its three-dimensional structure model was obtained. Mung bean trypsin inhibitor belongs to the most complex Bowman-Birk type inhibitor of serine protease inhibitors. The three-dimensional structure of this type of inhibitor has not been previously reported. The unit cell parameters of the MBILF-BTRY complex crystal are a = 62.99, b = 63.54, c = 69.70, α = β = γ = 90 °, space group P2_12_12_1, and the complex molecular weight is about 27500daltons. The independent diffraction spots with resolution of 3 were collected from 5142 Ru-300 X-ray machines and AFC-5 four-Park diffractometer. The coordinates of the bovine trypsin molecule obtained from the protein database are