Crystal structure of the nucleosome core particle at 2.8 Å resolution

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 a...

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Bibliographic Details
Published in:Nature (London) 1997-09, Vol.389 (6648), p.251-260
Main Authors: Richmond, Timothy J, Luger, Karolin, Mäder, Armin W, Richmond, Robin K, Sargent, David F
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Composition
Biological and medical sciences
Chromatin. Chromosome
Crystalline structure
Crystallography, X-Ray
DNA - chemistry
DNA, Superhelical - chemistry
Fundamental and applied biological sciences. Psychology
Histones - chemistry
Humanities and Social Sciences
Humans
Models, Molecular
Molecular and cellular biology
Molecular biophysics
Molecular genetics
Molecular Sequence Data
multidisciplinary
Nucleic Acid Conformation
Nucleosomes - chemistry
Protein Binding
Protein Conformation
Protein Folding
Science
Science (multidisciplinary)
Structure in molecular biology
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/38444