Crystallographic Structure of the Octameric Histone Core of the Nucleosome at a Resolution of 3.3 Å

• Published in: Science (American Association for the Advancement of Science) 1985-05, Vol.228 (4699), p.546-553
• Main Authors: Burlingame, Rufus W., Love, Warner E., Bi-Chen Wang Ron Hamlin, Xuong, Nguyen-Huu, Moudrianakis, Evangelos N.
• Format: Article
• Language: English
• Subjects: Animals; Atoms; Biochemistry; Biological and medical sciences; Cell organelles; Chickens; Chromatin; Chromatin - ultrastructure; Crystalline structure; Crystals; Dimers; DNA; DNA - metabolism; Electron density; Fundamental and applied biological sciences. Psychology; Histones; Histones - metabolism; Models, Chemical; Molecular biophysics; Nucleosomes; Nucleosomes - ultrastructure; Organelles; Protein Conformation; Solvents; Structure in molecular biology; X-Ray Diffraction
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.3983639

The structure of the (H2A-H2B-H3-H4)$_{2}$ histone octamer has been determined by means of x-ray crystallographic techniques at a resolution of 3.3 angstroms. The octamer is a prolate ellipsoid 110 angstroms long and 65 to 70 angstroms in diameter, and its general shape is that of a rugby ball. The size and shape are radically different from those determined in earlier studies. The most striking feature of the histone octamer is its tripartite organization, that is, a central (H3-H4)$_{2}$ tetramer flanked by two H2A-H2B dimers. The DNA helix, placed around the octamer in a path suggested by the features on the surface of the protein, appears like a spring holding the H2A-H2B dimers at either end of the (H3-H4)$_{2}$ tetramer.