| MWexperimental | 74 | kDa |
| MWexpected | 65 | kDa |
| VPorod | 107 | nm3 |
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log I(s)
2.32×103
2.32×102
2.32×101
2.32×100
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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) DOISASDNJ5 – Full length 3-phosphoinositide-dependent protein kinase (PDK1)
3-phosphoinositide-dependent protein kinase 1|
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Fits and models
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Synchrotron SAXS data from solutions of full length 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). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 10.00 μl sample at 6 mg/ml was injected at a 0.30 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Number of frames = UNKNOWN |
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