Structural mechanism of DNA recognition by the p204 HIN domain.

Fan X, Jiang J, Zhao D, Chen F, Ma H, Smith P, Unterholzner L, Xiao TS, Jin T, Nucleic Acids Res (2021) Europe PMC

SASDK92 – Interferon-activable protein 204 from Mus musculus (Mouse) amino-acids 215-619

Interferon-activable protein 204
MWI(0) 43 kDa
MWexpected 47 kDa
VPorod 28 nm3
log I(s) 1.07×102 1.07×101 1.07×100 1.07×10-1
Interferon-activable protein 204 small angle scattering data  s, nm-1
ln I(s)
Interferon-activable protein 204 Guinier plot ln 1.08×102 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
Interferon-activable protein 204 Kratky plot 1.104 0 √3 sRg
p(r)
Interferon-activable protein 204 pair distance distribution function Rg: 3.1 nm 0 Dmax: 9.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Interferon-activable protein 204 CHIMERA model
log I(s)
 s, nm-1
Interferon-activable protein 204 DAMMIF model
log I(s)
 s, nm-1
Interferon-activable protein 204 DAMMIF model
Synchrotron SAXS data from solutions of Interferon-activable protein 204 from Mus musculus (Mouse) amino-acids 215-619 in 20 mM HEPES, 100 mM KCl, pH 7.4 were collected on the X9A beam line at the National Synchrotron Light Source (NSLS) storage ring (Brookhaven, NY, USA) using a Pilatus 300K detector at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.80 mg/ml was measured at 25°C. 30 successive 2.300 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Sample detector distance = UNKNOWN. Concentration min = UNKNOWN

Interferon-activable protein 204 (p204 HINab)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Monomer
Mon. MW   46.6 kDa
 
UniProt   P0DOV2 (215-619)
Sequence   FASTA