The 2.5 Angstrom X-ray crystal structure of the nucleosome core particle pr
esented here provides significant additions to the understanding of the nuc
leosome, the fundamental unit of chromatin structure. Extensions are made t
o 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, whi
ch were expected to form a perfectly twofold symmetric nucleosome core part
icle. 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 latt
ice. An analysis is made of the asymmetries by comparisons both within the
nucleosome core particle and to the structure of the histone octamer core o
f the nucleosome.