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本文报道1.5分辨率去五肽(B26—B30)胰岛素结构的精化。用重新培养晶体所收集的衍射数据,约束参数最小二乘精化和模型重建工作交替进行。对2.4分辨率的原有模型作了广泛的精化,模型的某些部分作了较大的修正。晶体所含的镉配位结构已经很好地确定,它相当接近于一个理想的正八面体。精化后测定了84个水氧原子,为去五肽胰岛素晶体中水结构的研究提供了详细的信息.对于10—1.5分辨率范围内的5678个独立可观测(>1.5σ(F_0))反射,其最后的晶体学可靠性因子R为0.144;精化的模型同标准键长的均方根偏差为0.04。
This article reports the refinement of the insulin structure of the 1.5-deadened pentapeptide (B26-B30). Using the diffraction data collected from the recrystallization crystal, the least squares refinement of the constraint parameters and the model reconstruction work are alternated. The original model of 2.4 resolution has been extensively refined, and some parts of the model have been greatly revised. The crystal contains the coordination structure of cadmium has been well established, it is quite close to an ideal octahedron. The determination of 84 water-oxygen atoms after purification provides detailed information on the water structure in de-pentapeptide insulin crystals.For the 5678 independently observable (> 1.5σ (F_0)) in the 10-1.5 resolution range, Reflection, the final crystallographic reliability factor R is 0.144; the refined model has a root mean square deviation from the standard bond length of 0.04.