| MWexperimental | 101 | kDa |
| MWexpected | 100 | kDa |
| VPorod | 152 | nm3 |
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log I(s)
2.83×10-1
2.83×10-2
2.83×10-3
2.83×10-4
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s, nm-1
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14-3-3 protein inhibits CaMKK1 by blocking the kinase active site with its last two C-terminal helices.
Petrvalska O, Honzejkova K, Koupilova N, Herman P, Obsilova V, Obsil T, Protein Sci :e4805 (2023) Europe PMCSASDS46 – Human phosphorylated calcium/calmodulin-dependent protein kinase kinase 1 (CaMKK1) bound to 14-3-3 protein gamma
Calcium/calmodulin-dependent protein kinase kinase 1 (M474L)14-3-3 protein gamma
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Fits and models
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Synchrotron SAXS data from solutions of CaMKK1 bound to 14-3-3 protein gamma in 50 mM Tris-HCl, 150 mM NaCl, 1 mM TCEP, 3% (w/v) glycerol, pH 7.5 were collected on the P12 beam line at PETRAIII (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123983 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 25.5 mg/ml was injected at a 0.30 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 2400 successive 0.500 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.
Complex between phosphorylated human CaMKK1 and 14-3-3 gamma. Ab initio reconstruction was done by DAMMIF, 15 repetitions, slow mode, symmetry P1, averaged by DAMAVER and refined by DAMMIN. The DAMFILT model derived from the spatial alignment of the 15 models is also displayed. |
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