Summary information and primary citation
- PDB-id
-
1eqz;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- structural protein-DNA
- Method
- X-ray (2.5 Å)
- Summary
- X-ray structure of the nucleosome core particle at 2.5
Å resolution
- Reference
-
Harp JM, Hanson BL, Timm DE, Bunick GJ (2000): "Asymmetries
in the nucleosome core particle at 2.5 A resolution."
Acta Crystallogr.,Sect.D, 56,
1513-1534. doi: 10.1107/S0907444900011847.
- 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.