完全行列最小二乗法によるリゾチームの結晶構造精密化

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  • Full-Matrix Least-Squares Refinement of Lysozyme Crystal Structures.
  • カンゼン ギョウレツ サイショウ 2ジョウホウ ニ ヨル リゾチーム ノ ケッショウ コウゾウ セイミツカ

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Crystal structures of turkey and human lysozymes were refined at atomic resolution by full-matrix least-squares method with anisotropic temperature factors. The refinement converged at the R-value of 0.104 for turkey lysozyme and 0.115 for human lysozyme at 1.12 Å and 1.15 Å resolution, respectively, and the estimated r.m.s. coordinate errors for respective pro-teins were 0.031 Å and 0.034 Å. The magnitude and the degree of anisotropy of the atomic thermal motion have strong positive correlation with the square of distance from the molecular centroid. The statistical analysis suggested that such characteristics of anisotropic thermal motion are ascribed to the rigid-body rotation and local motions rather than the breathing motion.

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