Unveiling the dimer/monomer propensities of Smad MH1-DNA complexes

Ruiz L, Kaczmarska Z, Gomes T, Aragón E, Torner C, Freier R, Bagiński B, Martin-Malpartida P, de Martin Garrido N, Márquez J, Cordeiro T, Pluta R, Macias M, (2019) DOI

SASDE42 – Mothers against decapentaplegic homolog 8_9 - Smad8_9 MH1

Mothers against decapentaplegic homolog 8_9
MWexperimental 20 kDa
MWexpected 15 kDa
VPorod 34 nm3
log I(s) 1.64×101 1.64×100 1.64×10-1 1.64×10-2
Mothers against decapentaplegic homolog 8_9 small angle scattering data  s, nm-1
ln I(s)
Mothers against decapentaplegic homolog 8_9 Guinier plot ln 1.64×101 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
Mothers against decapentaplegic homolog 8_9 Kratky plot 1.104 0 √3 sRg
p(r)
Mothers against decapentaplegic homolog 8_9 pair distance distribution function Rg: 1.9 nm 0 Dmax: 6.5 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of mothers against decapentaplegic homolog 8_9 (Smad8_9 MH1) in 20 mM Tris 150 mM NaCl, pH 7.2 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-to-detector distance of 2.87 m and an X-ray wavelength, λ, of 0.09919 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 7.69 mg/ml was measured at 10°C. 10 successive 1 s 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. The data is recorded from a sample in monomer-dimer equilibrium.

Mothers against decapentaplegic homolog 8_9 (Smad8_9 MH1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Unknown
Mon. MW   14.7 kDa
 
UniProt   O15198 (16-141)
Sequence   FASTA