| MWexperimental | 78 | kDa |
| MWexpected | 76 | kDa |
| VPorod | 104 | nm3 |
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log I(s)
7.36×101
7.36×100
7.36×10-1
7.36×10-2
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s, nm-1
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Cryo-EM structures of Trypanosoma brucei gambiense ISG65 with human complement C3 and C3b and their roles in alternative pathway restriction.
Sülzen H, Began J, Dhillon A, Kereïche S, Pompach P, Votrubova J, Zahedifard F, Šubrtova A, Šafner M, Hubalek M, Thompson M, Zoltner M, Zoll S, Nat Commun 14(1):2403 (2023) Europe PMCSASDPA9 – invariant surface glycoprotein ISG65 bound to complement C3 (C3d)
65 kDa invariant surface glycoprotein, putativeComplement C3
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Fits and models
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Synchrotron SAXS data from solutions of invariant surface glycoprotein ISG65 bound to complement C3 (C3d) in 20 mM HEPES, 150 mM NaCl, 3% (v/v) glycerol, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.099 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 50.00 μl sample at 15 mg/ml was injected at a 0.08 ml/min flow rate onto a GE Superdex 200 Increase 3.2/300 column at 20°C. 1200 successive 1 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.
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