| 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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