1EQZ

X-RAY STRUCTURE OF THE NUCLEOSOME CORE PARTICLE AT 2.5 A RESOLUTION

Summary for 1EQZ

• Entry DOI: 10.2210/pdb1eqz/pdb
• Descriptor: 146 NUCLEOTIDES LONG DNA, PROTEIN (HISTONE H2A), PROTEIN (HISTONE H2B), ... (10 entities in total)
• Functional Keywords: nucleosome, nucleosome core particle, histone, microgravity histone octamer, dna palindrome, dna protein complex, chromatin, chromosomal protein, histone fold, bent dna, structural protein-dna complex, structural protein/dna
• Biological source: Gallus gallus (chicken); More
• Cellular location: Nucleus: P02263 P84229 P62801
• Total number of polymer chains: 10
• Total formula weight: 200891.62

Authors

Hanson, B.L.,Harp, J.M.,Timm, D.E.,Bunick, G.J. (deposition date: 2000-04-06, release date: 2000-04-17, Last modification date: 2023-08-09)

Primary citation

Harp, J.M.,Hanson, B.L.,Timm, D.E.,Bunick, G.J.
Asymmetries in the nucleosome core particle at 2.5 A resolution.
Acta Crystallogr.,Sect.D, 56:1513-1534, 2000

PubMed Abstract: The 2.5 A X-ray crystal structure of the nucleosome core particle presented here provides significant additions to the understanding of the nucleosome, the fundamental unit of chromatin structure. Extensions are made to the structure of the N-terminal histone tails and details are provided on hydration and ion binding. The structure is composed of twofold symmetric molecules, native chicken histone octamer cores and the DNA palindrome, which were expected to form a perfectly twofold symmetric nucleosome core particle. In fact, the result is asymmetric owing to the binding of the DNA to the protein surface and to the packing of the particles in the crystal lattice. An analysis is made of the asymmetries by comparisons both within the nucleosome core particle and to the structure of the histone octamer core of the nucleosome.

PubMed: 11092917
DOI: 10.1107/S0907444900011847

Experimental method

X-RAY DIFFRACTION (2.5 Å)