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
SASDV77 – Human Splicing Factor Proline/Glutamine rich SFPQ1 dimer with C-terminal truncation (delta599-707) in low salt buffer
Synchrotron SAXS
data from solutions of
Human Splicing Factor Proline/Glutamine rich SFPQ1 dimer with C-terminal truncation (delta599-707) in low salt buffer
in
150 mM KCl, 20 mM HEPES, 5% glycerol, 5 mM MgCl2, 1 mM DTT, pH 7.5
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 3 m and
at a wavelength of λ = 0.10781 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 4.91 mg/ml was measured
at 25°C.
400 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 the protein SFPQ(1-598) dialysed into a low salt buffer that appears to make the protein more compact than in a high salt buffer.
The experiment was carried out at the Australian Synchrotron SAXS/WAXS beamline with protein at 4.91 mg/ml in 150mM KCl, 20mM HEPES (pH 7.4), 5% glycerol, 5mM MgCl2, 1mM DTT.
This is part of the manuscript ' Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation '.
Porod and MW calculated using the Vp method https://doi.org/10.1002/pro.3528
s, nm-1
