Abstract
Dynamic structures of proteins derived from X-ray crystallography are described. A new method of dynamic structure refinement is proposed. In the method, 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 showed; (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.
