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Article
Nature 389, 251-260 (18 September 1997) | doi:10.1038/38444; Received 8 May 1997; Accepted 9 July 1997
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Crystal structure of the nucleosome core particle at 2.8 Å resolution
Karolin Luger1, Armin W. Mäder1, Robin K. Richmond1, David F. Sargent1 & Timothy J. Richmond1
- Institut für Molekularbiologie und Biophysik ETHZ, ETH-Hönggerberg, CH-8093 Zürich, Switzerland
Correspondence to: Timothy J. Richmond1 Correspondence and requests for materials should be addressed to T.J.R. The atomic coordinates have been deposited in the Brookhaven Protein Databank under code 1aoi.
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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