Evaluation of Molecular Perturbation of a Deuterated Protein by Temperature Factor Refinement in X-Ray Structural Analysis of High- Resolution Diffraction Data
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引用次数: 0
Abstract
Structural analysis of deuterated proteins, which are essential for neutron protein crystallography, involves refinement of X-ray crystallographic data using atomic or molecular thermal stability factors. Analysis of high resolution (~0.9 A) X-ray data can localize some of the hydrogen atoms in a protein molecule. Thermal stabilities and temperature factors are affected by some reasons; one of them is the masses of hydrogen and deuterium atoms. We propose a method to refine X-ray data, taking into account these effects, to show existence probability for deuterium in the protein. Thermal factors were calculated using several physical parameters, and the resultant values were fitted to the experimental thermal factors with high accuracy. This computational method can be applied to analyze and predict the hydrogen/deuterium exchanged states of protein crystals, even small crystals that are unsuitable for neutron crystallography.
氘化蛋白的结构分析是中子蛋白晶体学的基础,涉及到使用原子或分子热稳定因子对x射线晶体学数据进行细化。分析高分辨率(~0.9 A) x射线数据可以定位蛋白质分子中的一些氢原子。热稳定性和温度因子受各种原因的影响;其中之一是氢原子和氘原子的质量。我们提出了一种方法来细化x射线数据,考虑到这些影响,以显示氘在蛋白质中的存在概率。利用几种物理参数计算热因子,结果与实验热因子拟合精度较高。这种计算方法可以用于分析和预测蛋白质晶体的氢/氘交换态,甚至是不适合中子晶体学的小晶体。