Crystal structure of the nucleosome core particle at 2.8 Å resolution

@article{Luger1997CrystalSO,
  title={Crystal structure of the nucleosome core particle at 2.8 {\AA} resolution},
  author={Karolin Luger and Armin W. M{\"a}der and Robin K. Richmond and David F. Sargent and Timothy J. Richmond},
  journal={Nature},
  year={1997},
  volume={389},
  pages={251-260}
}
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… Expand
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TLDR
The crystal structure of the nucleosome core particle has been solved to 7 Å resolution and the central turn of superhelix and H3 · H4 tetramer have dyad symmetry, but the H2A · H2B dimers show departures due to interparticle associations. Expand
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Publisher Summary This chapter presents an account of the results of a low resolution study, by X-ray diffraction and electron microscopy, of single crystals of nucleosome cores from rat liverExpand
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TLDR
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