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Molecular dynamics studied by analysis of the X-ray diffuse scattering from lysozyme crystals

Nature volume 325, pages 643–646 (1987)Cite this article

Abstract

It is now well established that the biological activity of proteins is related not only to their mean molecular structure, but also to their intramolecular mobility1–4. Nearly all techniques sensitive to dynamics have given evidence for intramolecular mobility in proteins: NMR5,6, ESR7, Raman spectroscopy8,9, fluorescence quenching10, Mössbauer spectroscopy11, neutron scattering12, measurements of elastic constants13 and hydrogen–deuterium exchange14. The dynamics of proteins has also been approached by theoretical calculations15,16. We report here investigations of the atomic and molecular displacements in hen egg-white lysozyme crystals using a new technique. This technique, based on the X-ray diffuse scattering analysis (scattering out of the Bragg reflections), can yield information on the atomic displacements, provided that they are correlated. Rigid-body molecular displacements, correlated along short rows of aligned molecules in two perpendicular directions, have been detected and analysed (mean square amplitude of the order of 5 x 10-4 nm2). This technique can be also applied to the detection and analysis of intramolecular displacements.

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Authors and Affiliations

  1. LURE, Laboratoire CNRS-CEA-MEN, Bât. 209D, Université Paris-sud, Orsay, F-91405, France

    J. Doucet & J. P. Benoit

  2. Laboratoire de Physique des Solides, Bât. 510, Université Paris-sud, Orsay, F-91405, France

    J. Doucet

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  1. J. Doucet
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  2. J. P. Benoit
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Doucet, J., Benoit, J. Molecular dynamics studied by analysis of the X-ray diffuse scattering from lysozyme crystals. Nature 325, 643–646 (1987). https://doi.org/10.1038/325643a0

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