| MWexperimental | 56 | kDa |
| MWexpected | 55 | kDa |
| VPorod | 150 | nm3 |
|
log I(s)
4.13×10-3
4.13×10-4
4.13×10-5
4.13×10-6
|
s, nm-1
|
Structural insights into the multifunctionality of rabies virus P3 protein.
Sethi A, Rawlinson SM, Dubey A, Ang CS, Choi YH, Yan F, Okada K, Rozario AM, Brice AM, Ito N, Williamson NA, Hatters DM, Bell TDM, Arthanari H, Moseley GW, Gooley PR, Proc Natl Acad Sci U S A 120(14):e2217066120 (2023) Europe PMCSASDQJ4 – N226H Nishigahara Phosphoprotein Isoform 3 (N226H_P3)
Isoform P3 of Phosphoprotein Nish P3 N226H|
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Fits and models
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Rg, nm
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Synchrotron SAXS
data from solutions of
N226H Nishigahara Phosphoprotein Isoform 3 (N226H_P3)
in
25 mM HEPES, 150 mM NaCl, 1 mM TCEP, 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 3.3 m and
at a wavelength of λ = 0.103 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 5.00 mg/ml was measured
at 22°C.
One
1 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.
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