| MWexperimental | 34 | kDa |
| MWexpected | 32 | kDa |
| VPorod | 41 | nm3 |
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log I(s)
1.05×10-2
1.05×10-3
1.05×10-4
1.05×10-5
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s, nm-1
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The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement
Metcalfe R Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M, Journal of Biological Chemistry :jbc.RA119.012351 (2020) DOISASDGG2 – Interleukin 11 receptor subunit alpha
Interleukin-11 receptor subunit alpha|
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Fits and models
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Synchrotron SAXS data from solutions of the alpha subunit of the interleukin 11 receptor in 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH 8.5 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Dectris/Pilatus3 S 2M detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.1078 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 sample at 2.7 mg/ml was injected at a 0.45 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. Six successive 1 second frames were collected through the SEC elution peak of the sample. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Storage temperature = UNKNOWN. Sample injection volume = UNKNOWN |
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