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Crystallographic studies of the dynamic properties of lysozyme

Nature volume 280, pages 563–568 (1979)Cite this article

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.

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Authors and Affiliations

  1. Laboratory of Molecular Biophysics, Zoology Department, South Parks Road, Oxford, UK

    P. J. Artymiuk, C. C. F. Blake, D. E. P. Grace, S. J. Oatley, D. C. Phillips & M. J. E. Sternberg

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  1. P. J. Artymiuk
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  2. C. C. F. Blake
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  3. D. E. P. Grace
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  4. S. J. Oatley
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  5. D. C. Phillips
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  6. M. J. E. Sternberg
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Artymiuk, P., Blake, C., Grace, D. et al. Crystallographic studies of the dynamic properties of lysozyme. Nature 280, 563–568 (1979). https://doi.org/10.1038/280563a0

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