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Crystal structure of globular domain of histone H5 and its implications for nucleosome binding

Nature volume 362, pages 219–223 (1993)Cite this article

Abstract

The structure of GH5, the globular domain of the linker histone H5, has been solved to 2.5 Å resolution by multiwavelength anomalous diffraction on crystals of the selenomethionyl protein. The structure shows a striking similarity to the DNA-binding domain of the catabolite gene activator protein CAP, thereby providing a possible model for the binding of GH5 to DNA.

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Authors and Affiliations

  1. Biology Department, Brookhaven National Laboratory, Upton, New York, 11973, USA

    V. Ramakrishnan, V. Graziano, P. L. Lee & R. M. Sweet

  2. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    V. Ramakrishnan & J. T. Finch

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  1. V. Ramakrishnan
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  2. J. T. Finch
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  3. V. Graziano
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  4. P. L. Lee
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  5. R. M. Sweet
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Ramakrishnan, V., Finch, J., Graziano, V. et al. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 362, 219–223 (1993). https://doi.org/10.1038/362219a0

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