Crystal structure of the nucleosome core particle at 2.8 Å resolution

  title={Crystal structure of the nucleosome core particle at 2.8 {\AA} resolution},
  author={Karolin Luger and Armin W. M{\"a}der and Robin K. Richmond and David F. Sargent and Timothy J. Richmond},
The X-ray crystal structure of the nucleosome core particle of chromatin shows in atomic detail how the histone protein octamer is assembled and how 146 base pairs of DNA are organized into a superhelix around it. Both histone/histone and histone/DNA interactions depend on the histone fold domains and additional, well ordered structure elements extending from this motif. Histone amino-terminal tails pass over and between the gyres of the DNA superhelix to contact neighbouring particles. The… 

Asymmetries in the nucleosome core particle at 2.5 A resolution.

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.

The structure of DNA in the nucleosome core

Comparison of the 147-base-pair structure with two 146- base-pair structures reveals alterations in DNA twist that are evidently common in bulk chromatin, and which are of probable importance for chromatin fibre formation and chromatin remodelling.

DNA binding within the nucleosome core.

Cryo-EM of nucleosome core particle interactions in trans

The overall conformational flexibility of the NCP pair suggests that chromatin tertiary structure is dynamic and allows access of various chromatin modifying machineries to nucleosomes.

X-ray structure of the MMTV-A nucleosome core

This is the first nucleosome core particle structure containing a promoter sequence and crystallized from Mg2+ ions, which reveals sequence-dependent DNA conformations not seen previously, including kinking into the DNA major groove.

High resolution dynamic mapping of histone-DNA interactions in a nucleosome

A detailed map of histone-DNA interactions along the DNA sequence to near base pair accuracy is presented by mechanically unzipping single molecules of DNA, each containing a single nucleosome.



Structure of the nucleosome core particle at 7 Å resolution

The crystal structure of the nucleosome core particle has been solved to 7 Å resolution and the central turn of superhelix and H3 · H4 tetramer have dyad symmetry, but the H2A · H2B dimers show departures due to interparticle associations.

X-ray diffraction analysis of crystals containing twofold symmetric nucleosome core particles.

Nucleosome core particles containing a DNA palindrome and purified chicken erythrocyte histone octamer have been reconstituted and crystallized to ensure that the structure determined by X-ray diffraction will yield a true representation of the DNA strand rather than the twofold averaged structure which would result from using a non-palindromic DNA sequence.

Crystals of a nucleosome core particle containing defined sequence DNA.

Characterization of nucleosome core particles containing histone proteins made in bacteria.

Nucleosome core particles containing native and mutant histones made in bacteria have facilitated its X-ray structure determination at 2.8 A resolution.

The effect of nucleosome phasing sequences and DNA topology on nucleosome spacing.

It is found that nucleosome repeats directed by a strong positioning sequence are dominated by the cation-induced spacing as well as by the effects of topology, which is described as a new parameter that influences nucleosomal spacing in a predictable way.

The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix.

The structure of the octameric histone core of the nucleosome has been determined by x-ray crystallography to a resolution of 3.1 A and the folded histone chains are elongated rather than globular and are assembled in a characteristic "handshake" motif, which is named the histone fold.

Mapping nucleosome position at single base-pair resolution by using site-directed hydroxyl radicals.

A base-pair resolution method for determining nucleosome position in vitro has been developed to com- plement existing, less accurate methods and is potentially adaptable for determine nucleosomes position in chromatin in vivo.

Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin

It is concluded that H1 stabilizes the nucleosome and is located in the region of the exit and entry points of the DNA in H1-depleted chromatin, which has the form of an unravelled filament.

Sequence periodicities in chicken nucleosome core DNA.