去六肽（B25 - B30）胰岛素在0.25纳米分辨率下的晶体结构。

The crystal structure of deshexapeptide (B25-B30) insulin at 0.25 nm resolution.

作者信息

Chang W, Jiang T, Ren Z, Wan Z, Xu Y, Liang D, Zhu S, Zhang Y

机构信息

State key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.

出版信息

Sci China B. 1995 Sep;38(9):1094-100.

PMID:8554678

Abstract

The determination of deshexapeptide (B25-B30) insulin (DHI) was divided into two steps. At the first step, the rough structure model of DHI molecule was determined by using the molecular replacement method associated with the molecular close-packing method at 0.30 nm resolution based on the reflection data collected on four-cycle diffractometer. At the second step, the DHI model was adjusted and refined at 0.25 nm resolution based on the data collected on Area Detector. 40 water molecules were determined during the refinement, the final R-factor is 0.185 with R.M.S. deviation of 0.002 nm for bond lengths and 1.9 degrees for bond angles. The differences in conformation and function of DHI with other insulin analogues were compared and discussed.

摘要

去六肽（B25 - B30）胰岛素（DHI）的结构测定分为两步。第一步，基于在四圆衍射仪上收集的衍射数据，利用分子置换法结合分子密堆积法在0.30 nm分辨率下确定DHI分子的初步结构模型。第二步，基于在面探测器上收集的数据，在0.25 nm分辨率下对DHI模型进行调整和精修。精修过程中确定了40个水分子，最终的R因子为0.185，键长的均方根偏差为0.002 nm，键角的均方根偏差为1.9度。比较并讨论了DHI与其他胰岛素类似物在构象和功能上的差异。