Full-length SFPQ, and SFPQ1-598 homodimers

SASDV57 – Full-length SFPQ in high salt buffer

Splicing factor, proline- and glutamine-rich
MWexperimental 200 kDa
MWexpected 153 kDa
VPorod 485 nm3
log I(s) 2.59×10-2 2.59×10-3 2.59×10-4 2.59×10-5
Splicing factor, proline- and glutamine-rich small angle scattering data  s, nm-1
ln I(s)
Splicing factor, proline- and glutamine-rich Guinier plot ln 2.59×10-2 Rg: 7.9 nm 0 (7.9 nm)-2 s2
(sRg)2I(s)/I(0)
Splicing factor, proline- and glutamine-rich Kratky plot 1.104 0 3 sRg
p(r)
Splicing factor, proline- and glutamine-rich pair distance distribution function Rg: 9.5 nm 0 Dmax: 42.5 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Dimeric full-length human Splicing factor, proline- and glutamine-rich (SFPQ) in 500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTT, pH 7.4 were collected on the SAXS/WAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.10781 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 60.00 μl sample at 4.2 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 25°C. 450 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. A dimer of full-length SFPQ at 4.2mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. Measurement was taken at the Australian Synchrotron SAXS/WAXS beamline and is part of the manuscript ' Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation '.

A dimer of full-length SFPQ at 4.2mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. Measurement was taken at the Australian Synchrotron SAXS/WAXS beamline and is part of the manuscript ' Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation '.

Splicing factor, proline- and glutamine-rich (SFPQ cysteine dimer)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   76.3 kDa
 
UniProt   P23246 (214-707)
Sequence   FASTA