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Normal mode refinement: Crystallographic refinement of protein dynamic structure applied to human lysozyme
Author(s) -
Kidera Akinori,
Inaka Koji,
Matsushima Masaaki,
Gō Nobuhiro
Publication year - 1992
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360320404
Subject(s) - lysozyme , chemistry , anisotropy , debye–waller factor , normal mode , amplitude , crystallography , structure factor , molecular physics , physics , diffraction , optics , quantum mechanics , vibration , biochemistry
A new method of dynamic structure refinement of protein x‐ray crystallography, normal mode refinement; is developed. In this method the Debye–Waller factor is expanded in terms of the low‐frequency normal modes and external normal modes, whose amplitudes and couplings are optimized in the process of crystallographic refinement. By this method, internal and external contributions to the atomic fluctuations can be separated. Also, anisotropic atomic fluctuations and their interatomic correlations can be determined experimentally even with a relatively small number of adjustable parameters. The method is applied to the analysis of experimental data of human lysozyme to reveal its dynamic structure.