Molecular rigid-body displacements in a tetragonal lysozyme crystal confirmed by X-ray diffuse scattering.
X-ray diffuse scattering from protein crystals is, at the moment, the only available experimental process to be directly sensitive to long-range correlations between protein-atom displacements. It is shown here that calculations based on independent rigid-body displacements of individual molecules yield a description in good agreement with the experimental diffuse-scattering pattern displayed by tetragonal crystals of hen egg-white lysozyme (HEWL) In particular, it appears that molecular rigid-body translations and rigid- body rotations appear roughly in the same proportion as the average atomic mean-square positional fluctuations. The crystallographic temperature-factor analysis by TLS (translation/libration/screw) refinement, performed by Sternberg, Grace & Phillips [Sternberg, Grace, & Phillips (1979). J. Mol. Biol. 130, 231-253], is then confirmed and completed by a quantitative estimation of the molecular rigid-body translation contributions. The major contribution of molecular rigid- body displacements to the average atomic mean-square positional fluctuations, contradicts a previous analysis of the tetragonal HEWL diffuse-scattering data by Clarage, Clarage, Phillips, Sweet & Caspar [Clarage, Clarage, Phillips, Sweet & Caspar (1992). Proteins Struct. Funct. Genet. 12, 145-157] which concluded that short-range correlations dominate. The origin of these opposite conclusions mostly lies in the different hypotheses made to model diffuse scattering, underlying the limits of the 'homogeneous disorder' model.
LURE, Laboratoire CNRS-CEA-MENESR, Bâtiment 209D, Université Paris-Sud, Orsay, France. perez@lure.u-psud.fr
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Benoit