Kidera A, Go N
Protein Engineering Research Institute, Suita, Japan.
Proc Natl Acad Sci U S A. 1990 May;87(10):3718-22. doi: 10.1073/pnas.87.10.3718.
An x-ray crystallographic refinement method, referred to as the normal mode refinement, is proposed. The Debye-Waller factor is expanded in terms of the effective normal modes whose amplitudes and eigenvectors are experimentally determined by the crystallographic refinement. In contrast to the conventional method, the atomic motions are treated generally as anisotropic and concerted. This method is assessed by using the simulated x-ray data given by a Monte Carlo simulation of human lysozyme. In this article, we refine the dynamic structure by fixing the average static structure to exact coordinates. It is found that the normal mode refinement, using a smaller number of variables, gives a better R factor and more information on the dynamics (anisotropy and collectivity in the motion).
提出了一种X射线晶体学精修方法，称为正常模式精修。德拜-瓦勒因子根据有效正常模式展开，其振幅和本征向量通过晶体学精修实验确定。与传统方法不同，原子运动通常被视为各向异性且协同的。通过使用对人溶菌酶进行蒙特卡罗模拟给出的模拟X射线数据来评估该方法。在本文中，我们通过将平均静态结构固定到精确坐标来精修动态结构。结果发现，使用较少数量变量的正常模式精修给出了更好的R因子以及更多关于动力学的信息（运动中的各向异性和集体性）。
