SASDUV5 – Human Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) motif bound to 3'UTR fragment of ADP-ribosylation factor 1

MWexperimental 109 kDa MWexpected 96 kDa VPorod 139 nm3 log I(s) 5.85×10-1 5.85×10-2 5.85×10-3 5.85×10-4  s, nm-1 Log plot Log-Log plot

ln I(s) ln 5.86×10-1 Rg: 5.5 nm 0 (5.5 nm)-2 s2 (sRg)2I(s)/I(0) 1.104 0 √3 sRg p(r) Rg: 5.3 nm 0 Dmax: 16.1 nm

Fits and models

---

log I(s)  s, nm-1 +3 Δ/σ -3  s, nm-1 Fit validation Metric Value pcormap χ² 0.055 1.110 Worse Better

---

SAXS data from solutions of double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) motif bound to the 3'UTR fragment of ADP-ribosylation factor 1 in 50 mM TRIS, 300 mM NaCl, 3.8 mM β-mercaptoethanol, pH 7 were collected using a Rigaku BioSAXS-2000 instrument at CEITEC (Brno, Czech Republic) equipped with a Rigaku HyPix-3000 detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.20 mg/ml was measured at 20°C. One 3600 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

3'UTR fragment of ADP-ribosylation factor 1 (ARF1) Mol. type   RNA Organism   Homo sapiens Olig. state   Monomer Mon. MW   14.2 kDa Sequence   FASTA   Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) (Stau1dsRBD3endΔSSM) Mol. type   Protein Organism   Homo sapiens Olig. state   Dimer Mon. MW   40.7 kDa Sequence   FASTA