| MWexperimental | 66 | kDa |
| MWexpected | 55 | kDa |
| VPorod | 180 | nm3 |
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log I(s)
2.60×10-2
2.60×10-3
2.60×10-4
2.60×10-5
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s, nm-1
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Conformational dynamics, RNA binding, and phase separation regulate the multifunctionality of rabies virus P protein.
Rawlinson SM, Chakraborty S, Sethi A, David CT, Harrison AR, Bird LE, Rozario AM, Uthishtran S, Ardipradja K, Zhao T, Oksayan S, Jans DA, Ang CS, Lu ZH, Yan F, Williamson NA, Arumugam S, Sundaramoorthy V, Bell TDM, Gooley PR, Moseley GW, Nat Commun 16(1):9491 (2025) Europe PMCSASDRZ4 – K214/R260 mutant of Rabies virus CVS Phosphoprotein Isoform 3 (KRm CVS P3)
Phosphoprotein (Isoform P3; K214A, R260A, D289N, C297S)|
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Fits and models
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Synchrotron SAXS data from solutions of the K214/R260 mutant of rabies virus CVS Phosphoprotein Isoform 3 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 (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 3.3 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) co-flow (sheath) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 5 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superose 6 Increase 5/150 column 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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