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

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 mobility. Nearly all techniques sensitive to dynamics have given evidence for intramolecular mobility in proteins: NMR, ESR, Raman spectroscopy, fluorescence quenching, Mössbauer spectroscopy, neutron scattering, measurements of elastic constants and hydrogen-deuterium exchange. The dynamics of proteins has also been approached by theoretical calculations. 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.