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1IWZ

Crystal Structure Analysis of Human lysozyme at 178K.

Summary for 1IWZ
Entry DOI10.2210/pdb1iwz/pdb
Related1IWT 1IWU 1IWV 1IWW 1IWX 1IWY
DescriptorLYSOZYME C, CHLORIDE ION (3 entities in total)
Functional Keywordso-glycosyl, glycosydase, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P61626
Total number of polymer chains1
Total formula weight14827.05
Authors
Joti, Y.,Nakasako, M.,Kidera, A.,Go, N. (deposition date: 2002-06-03, release date: 2002-09-04, Last modification date: 2024-11-20)
Primary citationJoti, Y.,Nakasako, M.,Kidera, A.,Go, N.
Nonlinear temperature dependence of the crystal structure of lysozyme: correlation between coordinate shifts and thermal factors.
Acta Crystallogr.,Sect.D, 58:1421-1432, 2002
Cited by
PubMed 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.
PubMed: 12198298
DOI: 10.1107/S0907444902011277
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.48 Å)
Structure validation

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