| MWexperimental | 32 | kDa |
| MWexpected | 35 | kDa |
| VPorod | 57 | nm3 |
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log I(s)
1.76×103
1.76×102
1.76×101
1.76×100
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s, nm-1
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Modulation of the substrate specificity of the kinase PDK1 by distinct conformations of the full-length protein
Sacerdoti M, Gross L, Riley A, Zehnder K, Ghode A, Klinke S, Anand G, Paris K, Winkel A, Herbrand A, Godage H, Cozier G, Süß E, Schulze J, Pastor-Flores D, Bollini M, Cappellari M, Svergun D, Gräwert M, Aramendia P, Leroux A, Potter B, Camacho C, Biondi R, Science Signaling 16(789) (2023) DOISASDNL5 – Double mutant catalytic domain of 3-phosphoinositide-dependent protein kinase 1 (PDK1 50–359; Y188G Q292A)
3-phosphoinositide-dependent protein kinase 1 (Y188G Q292A)|
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Fits and models
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Synchrotron SAXS data from solutions of the double mutant catalytic domain of PDK1 in 20 mM Tris-HCl pH 7.4, 250 mM NaCl, 1 mM DTT, 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 2.00 mg/ml was measured at 20°C. Five successive 0.100 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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