基準振動を用いたタンパク質の動的構造の結晶学の精密化
1992 年 34 巻 3 号 p. 186-191
詳細
1992 年 34 巻 3 号 p. 186-191
A dynamic structure refinement method for protein X-ray crystallography is presented. The Debye-Waller factor is expanded in terms of the low-frequency normal modes whose amplitudes and eigenvectors are experimentally optimized in the process of the crystallographic refinement.
Application of the method to human lysozyme showd: (1) Debye-Waller factor consists of two parts, highly anisotropic internal fluctuations and almost isotropic external terms. The former is smaller than the latter. (2) Correlation of fluctuations corresponding to the hinge-bending motion was detected.
