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去B链羧端六肽胰岛素(DHI)的结构测定是分两个阶段完成的.第一阶段是基于四圆衍射仪收集的数据,使用分子置换法和分子密堆积法确定0.30nm分辨率的初始结构模型;第二阶段是以X-200B面探测仪收集的衍射数据为基础完成0.25nm分辨率模型的调整和精化,精化过程中确定了与蛋白质紧密结合的40个水分子,最终R因子为18.5％,键长和键角的标准偏差分别为0.002m和1.9°.文中对DHI与其它胰岛素类似物的构象及功能的差异进行了比较和讨论.
The structural determination of the carboxy terminal hexapeptide insulin (DHI) to the B chain was performed in two stages: the first stage was based on the data collected by the four-circle diffractometer and molecular resolution and molecular close stacking were used to determine the resolution of 0.30 nm Initial structure model; the second stage is based on the diffraction data collected by the X-200B surface detector to complete the adjustment and refinement of 0.25nm resolution model, the process of refining identified 40 water molecules tightly bound to the protein, the final The R factor was 18.5%, and the standard deviation of bond length and bond angle was 0.002 m and 1.9 °, respectively. The differences in conformation and function between DHI and other insulin analogues were compared and discussed.