The Crystal Structure of the Nucleosome Core Particle by Contrast Variation

  • Graham A. Bentley
  • John T. Finch
  • Anita Lewit-Bentley
  • Michel Roth
Part of the Basic Life Sciences book series (BLSC, volume 27)


The nucleosome core particle may be regarded as a basic structural unit of chromatin and thus of the chromosome. It is obtained by micrococcal nuclease digestion of chromatin and consists of about equal weights of DNA (146 base pairs) and protein (an octamer of two pairs each of the histones H2A, H2B, H3, and H4). Nucleosome structure has been reviewed by McGhee and Felsenfeld (6). Studies by small-angle neutron scattering using D2O/H2O contrast variation have given the overall dimensions of the nucleosome and have shown that the protein forms an inner core with the DNA located at the outer regions of the molecule (7,12). The x-ray crystal structure of the nucleosome core particle has been solved in projection to a resolution of about 25 Å (3). Although this has given a more detailed description of the overall shape of the molecule than has solution scattering, the distinction between protein and DNA is not made. In this paper we show how the principle of contrast variation can be used in low resolution neutron diffraction to achieve this end.


Structure Factor Histone Core Contrast Variation Basic Structural Unit Scatter Length Density 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Bentley, G.A., Finch, J.T., and Lewit-Bentley, A., J. Mol. Biol. 145:771 (1981).PubMedCrossRefGoogle Scholar
  2. 2.
    Finch, J.T., Lutter, L.C., Rhodes, D., Brown, R.S., Rushton, B., and Klug, A., FEBS Symp. 51:193 (“Gene Functions,” FEBS 12th Meet., Dresden, 1978, S. Rosenthal et al., eds.), Pergamon, Oxford, 1979.Google Scholar
  3. 3.
    Finch, J.T., Lutter, L.C., Rhodes, D., Brown, R.S., Rushton, B., Levitt, M., and Klug, A., Nature 269:29 (1977).PubMedCrossRefGoogle Scholar
  4. 4.
    Finch, J.T., Brown, R.S., Rhodes, D., Richmond, T., Rushton, B., Lutter, L.C., and Klug, A., J. Mol. Biol. 145:757 (1981).PubMedCrossRefGoogle Scholar
  5. 5.
    Klug, A., Rhodes, D., Smith, J., Finch, J.T., and Thomas, J.O., Nature 287:509 (1980).PubMedCrossRefGoogle Scholar
  6. 6.
    McGhee, J.D. and Felsenfeld, G., Annu. Rev. Biochem. 49:1115 (1980).PubMedCrossRefGoogle Scholar
  7. 7.
    Pardon, J.F., Worcester, D.L., Wooley, J.C., Cotter, R.I., Lilley, D.M.J., and Richards, B.M., Nucl. Acids Res. 4:3199 (1977).PubMedCrossRefGoogle Scholar
  8. 8.
    Roth, M. and Lewit-Bentley, A., Acta Crystallogr. A38:670 (1982).Google Scholar
  9. 9.
    Sayre, D., Acta Crystallogr. 5:60 (1952).CrossRefGoogle Scholar
  10. 10.
    Sayre, D., Acta Crystallogr. A28:210 (1972).Google Scholar
  11. 11.
    Sayre, D., Acta Crystallogr. A30:180 (1974).Google Scholar
  12. 12.
    Suau, P., Kneale, G.G., Braddock, G.W., Baldwin, J.P., and Bradbury, E.M., Nucl. Acids Res. 4:3769 (1977).PubMedCrossRefGoogle Scholar
  13. 13.
    Worcester, D.L. and Franks, N.P., J. Mol. Biol. 100:359 (1976).PubMedCrossRefGoogle Scholar
  14. 14.
    Roth, M., Lewit-Bentley, A., and Bentley, G.A., Manuscript in preparation.Google Scholar

Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Graham A. Bentley
    • 1
  • John T. Finch
    • 2
  • Anita Lewit-Bentley
    • 1
  • Michel Roth
    • 3
  1. 1.EMBL Grenoble OutstationGrenoble CedexFrance
  2. 2.MRC Lab. of Molecular BiologyCambridgeEngland
  3. 3.Institut Laue-LangevinGrenoble CedexFrance

Personalised recommendations