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