2000/12/01 by Joel M. Harp, B. Leif Hanson, David E. Timm +1 · 7 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · #Biochemistry #Biology #Biophysics #Chemistry #Chromatin #Chromatosome #Crystallography #DNA #DNA and Nucleic Acid Chemistry #Genomics and Chromatin Dynamics #Histone #Histone H1 #Histone code #Histone octamer #Linker DNA #Nucleosome #Physics #Quantum mechanics #RNA and protein synthesis mechanisms #Solenoid
paper · doi:10.1107/s0907444900011847
openalex publication_date 2000/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
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.