| MWexperimental | 243 | kDa |
| MWexpected | 187 | kDa |
| VPorod | 357 | nm3 |
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log I(s)
9.65×10-2
9.65×10-3
9.65×10-4
9.65×10-5
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s, nm-1
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Cryo-EM analysis of complement C3 reveals a reversible major opening of the macroglobulin ring.
Gadeberg TAF, Jørgensen MH, Olesen HG, Lorentzen J, Harwood SL, Almeida AV, Fruergaard MU, Jensen RK, Kanis P, Pedersen H, Tranchant E, Petersen SV, Thøgersen IB, Kragelund BB, Lyons JA, Enghild JJ, Andersen GR, Nat Struct Mol Biol (2025) Europe PMCSASDTU8 – Complement C3* at 1.25 mg/mL (pH 6.0, 200 mM NaCl)
Complement C3 (Δ668-671)|
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Fits and models
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Synchrotron SAXS data from solutions of complement C3* in 20 mM MES pH 6.0, 200 mM NaCl, pH 6 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.25 mg/ml was measured at 8°C. 40 successive 0.095 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.
CAUTION! The low-angle SAXS intensities encompassing the entire Guinier region - and beyond to higher angle - (0.03 < s < 0.34 nm-1) have been removed when assessing the model fit to the data. Consequently, the model fit and particle sizing cannot be validated (e.g., Rg(model) = 4.8 nm; Rg(experiment) = 5.5 nm; Dmax model = 14.6 nm; Dmax(experiment) = 21.8 nm, etc). |
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