Nonlinear temperature dependence of the crystal structure of lysozyme: Correlation between coordinate shifts and thermal factors

Yasumasa Joti, Masayoshi Nakasako, Akinori Kidera, Nobuhiro Go

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

The static and dynamic structures of human lysozyme at seven different temperatures ranging from 113 to 178 K were investigated by normal-mode refinement of the cryogenic X-ray diffraction data collected from a single crystal. Normal-mode refinement decomposes the mean-square fluctuations of protein atoms from their average position into the contributions from the internal degrees of freedom, which change the shape of the protein structure, and those from the external degrees of freedom, which generate rigid-body motions in the crystal. While at temperatures below 150 K the temperature dependence of the total mean-square fluctuations shows a small gradient similar to that predicted theoretically by normal-mode analysis, at temperatures above 150 K there is an apparent inflection in the temperature dependence with a higher gradient. The inflection in the temperature dependence at temperatures above 150 K occurs mostly in the external degrees of freedom. Possible causes for the dynamic transition are discussed with respect to the crystal packing and physicochemical properties of crystalline water.

Original languageEnglish
Pages (from-to)1421-1432
Number of pages12
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number9
DOIs
Publication statusPublished - 2002 Sep 1
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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