Premium
Neutron scattering from chromatin in relation to higher‐order structure
Author(s) -
Baldwin J. P.,
Carpenter B. G.,
Crespi H.,
Hancock R.,
Stephens R. M.,
Simpson J. K.,
Bradbury E. M.,
Ibel K.
Publication year - 1978
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889878013667
Subject(s) - chromatin , histone , dna , chemistry , histone h1 , crystallography , biophysics , nucleosome , biology , biochemistry
Chromatin fibres containing histone H1 as well as the DNA and histones H2 A , H2 B , H3 and H4 show the same off‐meridional diffraction maxima at ~ 10 nm as reported by Carpenter, Baldwin, Bradbury & Ibel [ Nucleic Acids Res. (1976), 3 , 1739–1746] for chromatin fibres depleted of histone HI. It is shown that the intensity of the maximum (as a function of solvent scattering‐length density and deuteration of histones and DNA) can be quantitatively explained in terms of a globular protein component to the chromatin subunits in a matrix of hydrated DNA. The off‐meridional diffraction maximum suggests that the chromatin is in the form of a flat helix and clearly the relative amounts of protein and hydrated DNA vary along the length of the chromatin fibre.