应用差值Fourier技术,制约立体化学参数的最小二乘技术并辅以电子密度图的人工拟合,以0.25nm分辨率的去B链羧端六肽胰岛素(DHI)为起点,精化了0.15nm分辨率去六肽胰岛素的晶体结构,精化过程中确定了与蛋白质紧密结合的54个水分子。最终模型的晶体学可靠性只因子为0.187,键长和键角同标准值的均方根偏差分别为0.0016nm和2.7°。文中对DHI与其它胰岛素类似物的构象与功能差异进行了讨论。 The differential Fourier technique, the least squares technique for controlling the stereochemical parameters and the artificial fitting of the electron density map were used to refine the 0.15% de-B chain carboxy-terminal hexapeptide insulin (DHI) nm resolution to the hexapeptide insulin crystal structure, identified during the purification of protein in close contact with the 54 water molecules. The final model has a crystallographic reliability factor of only 0.187. The root mean square deviation of the bond length and bond angle from the standard values ​​is 0.0016 nm and 2.7 °, respectively. The conformational and functional differences between DHI and other insulin analogues are discussed.