Crystallographic studies of the dynamic properties of lysozyme
- 1 August 1979
- journal article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 280 (5723), 563-568
- https://doi.org/10.1038/280563a0
Abstract
The patterns of atomic displacements in the crystals of hen and human lysozyme derived from independent crystallographic refinement are broadly similar. Analysis of the pattern indicates a close correlation with molecular structure, strongly suggestive of intramolecular motion. The active site of lysozyme is located in a region of high displacement. It is concluded that protein mobility may play a significant part in biological activity and that X-ray crystallography can contribute to its analysis.Keywords
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