Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation

Koning H, Lai V, Sethi A, Chakraborty S, Ang C, Fox A, Duff A, Whitten A, Marshall A, Bond C, Acta Crystallographica Section D Structural Biology 81(7):357-379 (2025) DOI

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