Science · 1986 · 12 citations · 14 references
Life SciencesBiophysicsMolecular BiologyChromatin StructureMolecular BiophysicsStructural BiologyChromatinCrystallographyHistone ProteinsNucleosome StructureProtein ConformationX-ray CrystallographyAmmonium Sulfate PrecipitationDna Wrapping Around NucleosomesHistone Core StructureHistone Octamer OrganizationNucleosome Core Particle Structure
The conformation of the histone octamer is shown to depend upon the specific salt used to solubilize it. In 2M sodium chloride the octamer is similar in size and shape to the histone component of crystallized core nucleosomes. In contrast, in 3.5M ammonium sulfate the octamer is elongated, resembling an ellipsoid with approximate dimensions of 114 by 62 by 62 angstroms. These results indicate that the elongated conformation seen in the 3.3 angstroms electron density map of the histone octamer crystallized in ammonium sulfate is due to the particular salt conditions used.
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Structure of the nucleosome core particle at 7 Å resolution
Timothy J. Richmond, J.T. Finch, B. Rushton et al. · Nature · 1984 · 1K citations
A low resolution structure for the histone core of the nucleosome
A. Klug, Daniela Rhodes, Judith Smith et al. · Nature · 1980 · 307 citations
Conformational states of chromatin в bodies induced by urea
Donald E. Olins, Philip N. Bryan, Rodney E. Harrington et al. · Nucleic Acids Research · 1977 · 103 citations · Full text