Solution structure(s) of trinucleosomes from contrast variation SAXS

Mauney A, Muthurajan U, Luger K, Pollack L, Nucleic Acids Research (2021) DOI

SASDJ96 – Trinucleosomes from Xenopus laevis (African clawed frog)

Histone H3
Histone H4
Histone H2A type 1
Histone H2B
Non-linker Ended Trinucleosome DNA
MWexperimental 186 kDa
MWexpected 227 kDa
log I(s) 4.51×101 4.51×100 4.51×10-1 4.51×10-2
Histone H3 Histone H4 Histone H2A type 1 Histone H2B Non-linker Ended Trinucleosome DNA small angle scattering data  s, nm-1
ln I(s)
Histone H3 Histone H4 Histone H2A type 1 Histone H2B Non-linker Ended Trinucleosome DNA Guinier plot ln 4.51×101 Rg: 12.9 nm 0 (12.9 nm)-2 s2
(sRg)2I(s)/I(0)
Histone H3 Histone H4 Histone H2A type 1 Histone H2B Non-linker Ended Trinucleosome DNA Kratky plot 1.104 0 3 sRg
p(r)
Histone H3 Histone H4 Histone H2A type 1 Histone H2B Non-linker Ended Trinucleosome DNA pair distance distribution function Rg: 13.5 nm 0 Dmax: 41.8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Trinucleosomes from Xenopus laevis (African clawed frog) in 20 mM Tris 150 mM NaCl 1 mM EDTA 1 mM DTT 50% w/v sucrose, pH 7.5 were collected on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS) storage ring (Ithaca, NY, USA) using a Pilatus 200K detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.111 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.83 mg/ml was measured at 20°C. 70 successive 5 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Storage temperature = UNKNOWN

Histone H3
Mol. type   Protein
Organism   Xenopus laevis
Olig. state   Monomer
Mon. MW   15.4 kDa
 
UniProt   Q92133
Sequence   FASTA
 
Histone H4
Mol. type   Protein
Organism   Xenopus laevis
Olig. state   Monomer
Mon. MW   11.4 kDa
 
UniProt   P62799
Sequence   FASTA
 
Histone H2A type 1
Mol. type   Protein
Organism   Xenopus laevis
Olig. state   Monomer
Mon. MW   14.0 kDa
 
UniProt   P06897
Sequence   FASTA
 
Histone H2B
Mol. type   Protein
Organism   Xenopus laevis
Olig. state   Monomer
Mon. MW   13.9 kDa
 
UniProt   Q92130
Sequence   FASTA
 
Non-linker Ended Trinucleosome DNA
Mol. type   DNA
Olig. state   Monomer
Mon. MW   172.5 kDa
Sequence   FASTA