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Crystal structure of the nucleosome core particle at 2.8 Å resolution

Naturevolume 389, pages251–260 (1997)Cite this article

Abstract

The X-ray crystal structure of the nucleosome core particle of chromatin shows in atomic detail how the histone protein octamer is assembled and how 146 base pairs of DNA are organized into a superhelix around it. Both histone/histone and histone/DNA interactions depend on the histone fold domains and additional, well ordered structure elements extending from this motif. Histone amino-terminal tails pass over and between the gyres of the DNA superhelix to contact neighbouring particles. The lack of uniformity between multiple histone/DNA-binding sites causes the DNA to deviate from ideal superhelix geometry.

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Figure 1: Nucleosome core particle: ribbon traces for the 146-bp DNA phosphodiester backbones (brown and turquoise) and eight histone protein main chains (blue: H3; green: H4; yellow: H2A; red: H2B.
Figure 2: H3–H4 histone-fold pair.
Figure 3: Histone tails between DNA gyres.
Figure 4: Central DNA base pairs.

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Acknowledgements

We thank S. Halford for the EcoRV enzyme; A. Flaus, T. Rechsteiner and S. Tan for support and discussion; and C. Riekel and his co-workers at ID13 of the ESRF, Grenoble for support and cooperation. This research was supported in part by the Swiss National Fond.

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  1. Institut für Molekularbiologie und Biophysik ETHZ, ETH-Hönggerberg, CH-8093, Zürich, Switzerland

    Karolin Luger, Armin W. Mäder, Robin K. Richmond, David F. Sargent & Timothy J. Richmond

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Luger, K., Mäder, A., Richmond, R.et al. Crystal structure of the nucleosome core particle at 2.8 Å resolution.Nature389, 251–260 (1997). https://doi.org/10.1038/38444

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