| MWexperimental | 102 | kDa |
| MWexpected | 109 | kDa |
| VPorod | 443 | nm3 |
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log I(s)
8.94×103
8.94×102
8.94×101
8.94×100
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s, nm-1
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Preorganized cyclic modules facilitate the self-assembly of protein nanostructures
Snoj J, Lapenta F, Jerala R, Chemical Science (2024) DOISASDUR2 – SB24-nnn (coiled coil protein origami irregular octahedron assembled from three linear chains)
SB6 (Linear coiled-coil protein origami structure consisting of 6 coiled-coil forming segments)SB9b (Linear coiled-coil protein origami structure consisting of 9 coiled-coil forming segments)
SB9c (Linear coiled-coil protein origami structure consisting of 9 coiled-coil forming segments)
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Fits and models
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Synchrotron SAXS data from solutions of SB24-nnn in 20 mM Tris, 150 mM NaCL, 3% glycerol, pH 7.5 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). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 90.00 μl sample at 9.6 mg/ml was injected at a 0.75 ml/min flow rate onto a Cytiva Superdex 200 10/300 column at 20°C. 3000 successive 0.995 second frames were collected through the entire SEC elution. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
The experimental molecular weight quoted in this entry was evaluated using SEC-MALS combined with the refractive index (RI) measured before the SAXS measurements. |
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