title: Normal mode refinement: crystallographic refinement of protein dynamic structure. II. Application to human lysozyme.
abstract: The dynamic structure of a protein, human lysozyme, is determined by the normal mode refinement of X-ray crystal structure. This method uses the normal modes of both internal and external motions to distinguish the real internal dynamics from the external terms such as lattice disorder, and gives an anisotropic and concerted picture of atomic fluctuations. The refinement is carried out with diffraction data of 5.0 to 1.8 A resolution, which are collected on an imaging plate. The results of the refinement show: (1) Debye-Waller factor consists of two parts, highly anisotropic internal fluctuations and almost isotropic external terms. The former is smaller than the latter by a factor of 0.72 in the scale of B-factor. Therefore, the internal dynamics cannot be recognized directly from the apparent electron density distribution. (2) The internal fluctuations show basically similar features as those predicted by the normal mode analysis, with almost the same amplitude and a similar level of anisotropy. (3) Correlations of fluctuations are detected between two lobes forming the active site cleft, which move simultaneously in opposite directions. This corresponds to the hinge-bending motion of lysozyme.
authors.affiliation: Protein Engineering Research Institute, Osaka, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Kidera
authors.forename: K
authors.initials: K
authors.lastname: Inaka
authors.forename: M
authors.initials: M
authors.lastname: Matsushima
authors.forename: N
authors.initials: N
authors.lastname: Go
mesh_terms: D006801:Humans; D008433:Mathematics; D008958:Models, Molecular; D009010:Monte Carlo Method; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D012984:Software; D014961:X-Ray Diffraction / Q000379:methods*
chemical_list: D009113:Muramidase