Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein.

Hollmann NM, Jagtap PKA, Linse JB, Ullmann P, Payr M, Murciano B, Simon B, Hub JS, Hennig J, Nucleic Acids Res (2023) Europe PMC

SASDHL7 – Upstream of N-ras, isoform A, CSD 4 to 9 from Drosophila melanogaster

Upstream of N-ras, isoform A
MWexperimental 63 kDa
MWexpected 63 kDa
VPorod 136 nm3
log I(s) 5.82×101 5.82×100 5.82×10-1 5.82×10-2
Upstream of N-ras, isoform A small angle scattering data  s, nm-1
ln I(s)
Upstream of N-ras, isoform A Guinier plot ln 5.83×101 Rg: 4.9 nm 0 (4.9 nm)-2 s2
(sRg)2I(s)/I(0)
Upstream of N-ras, isoform A Kratky plot 1.104 0 3 sRg
Dmax: 25 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Unr CSD 4-9 in 20 mM HEPES, 150 mM NaCl, 1 mM DTT, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.0992 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.8 and 4.2 mg/ml were measured at 20°C. 10 successive 1 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.

Upstream of N-ras, isoform A (Unr)
Mol. type   Protein
Olig. state   Monomer
Mon. MW   63.1 kDa
 
UniProt   Q9VSK3 (429-990)
Sequence   FASTA