International
Tables for Crystallography Volume F Crystallography of biological macromolecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 19.4, p. 443
Section 19.4.6.1. Contrast variation
aDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA, and bDepartments of Chemistry and Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA |
An early result that changed ideas about nucleosome organization came from measurements relying on the difference in protein and DNA densities (Baldwin et al., 1975; Bradbury et al., 1976
). Information on the organization of serum lipoproteins was also based on intrinsic scattering differences (Stuhrmann et al., 1975
; Atkinson & Shipley, 1984
). The contrast between RNA and protein was used in early ribosome measurements (Crichton et al., 1977
; Moore et al., 1974
). Recent examples include detergent binding to membrane proteins (Timmins et al., 1991
) and the study of membrane protein–lipid complexes (Jeanteur et al., 1994
). Elegant use of contrast variation resulted in a structural explanation of the anti-cooperative binding of tRNA to synthetase, which had resisted study by other methods (Dessen et al., 1978
).
References








