REFINEMENT OF PROTEIN DYNAMIC STRUCTURE - NORMAL MODE REFINEMENT
REFINEMENT OF PROTEIN DYNAMIC STRUCTURE - NORMAL MODE REFINEMENT
复制标题
DOI：
10.1073/pnas.87.10.3718
复制
发表时间：
1990-05-01
影响因子：
11.1
通讯作者：
GO, N
中科院分区：
文献类型：
--
作者：
KIDERA, A;GO, N
提出了一种X射线晶体学细化方法，称为简正模细化。德拜-沃勒因子的有效的正常模式，其振幅和本征矢量是由晶体学的细化实验确定的方面展开。与传统的方法不同，该方法将原子的运动视为各向异性的协调运动。这种方法是通过使用模拟的X射线数据由Monte Carlo模拟人溶菌酶进行评估。在本文中，我们通过将平均静态结构固定到精确坐标来细化动态结构。据发现，正常模式的细化，使用较少的变量，给出了更好的R因子和更多的信息的动态（各向异性和集体的运动）。
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).