Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6JR1

Crystal structure of the human nucleosome phased with 16 selenium atoms

Summary for 6JR1
Entry DOI10.2210/pdb6jr1/pdb
DescriptorHistone H3.1, Histone H4, Histone H2A type 1-B/E, ... (8 entities in total)
Functional Keywordsnucleosome, chromatin, histone, selenomethionine, sad phasing, gene regulation, gene regulation-dna complex, gene regulation/dna
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains10
Total formula weight203988.01
Authors
Saotome, M.,Horikoshi, N.,Urano, K.,Kujirai, T.,Yuzurihara, H.,Kurumizaka, H.,Kagawa, W. (deposition date: 2019-04-02, release date: 2019-10-02, Last modification date: 2024-10-09)
Primary citationSaotome, M.,Horikoshi, N.,Urano, K.,Kujirai, T.,Yuzurihara, H.,Kurumizaka, H.,Kagawa, W.
Structure determination of the nucleosome core particle by selenium SAD phasing.
Acta Crystallogr D Struct Biol, 75:930-936, 2019
Cited by
PubMed Abstract: The eukaryotic genome is compacted inside the nucleus of the cell in the form called chromatin. The fundamental unit of chromatin is the nucleosome, which contains four types of histones (H3, H4, H2A and H2B) and approximately 150 base pairs of DNA wrapped around the histone complex. The structure of the nucleosome is highly conserved across several eukaryotic species, and molecular replacement has been the primary phasing method used to solve nucleosome structures by X-ray crystallography. However, there is currently no simple, widely applicable experimental phasing method for the nucleosome. In the present study, it is demonstrated that selenomethionine-incorporated histones H3, H2A and H2B can be reconstituted into nucleosomes and crystallized for structural determination. Unexpectedly, it was found that the nucleosome can be phased with a relatively small number of Se atoms. The structures of nucleosome core particles containing 12 and 16 Se atoms were solved by SAD phasing at 2.5 and 2.4 Å resolution, respectively. The present study demonstrates a simple method for determining nucleosome structures by experimental phasing, which may be particularly useful for noncanonical structures that cannot be solved by molecular replacement.
PubMed: 31588924
DOI: 10.1107/S2059798319012713
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon