| MWexperimental | 119 | kDa |
| MWexpected | 118 | kDa |
| VPorod | 207 | nm3 |
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log I(s)
8.57×104
8.57×103
8.57×102
8.57×101
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s, nm-1
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Conformational States of Exchange Protein Directly Activated by cAMP (EPAC1) Revealed by Ensemble Modeling and Integrative Structural Biology.
White MA, Tsalkova T, Mei FC, Cheng X, Cells 9(1) (2019) Europe PMCSASDCS6 – Rap guanine nucleotide exchange factor 3 (isoform3) bound to RAS related protein 1b - with cAMP
Rap guanine nucleotide exchange factor 3RAS related protein 1b
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Fits and models
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SAXS data from solutions of Rap guanine nucleotide exchange factor 3 (isoform3) bound to RAS related protein 1b - with cAMP - in 1mM EDTA, 10mM DTT, 500mM NaCl, 1mM cAMP, 10mM Tris, pH 9 were collected using a Rigaku BioSAXS-1000 instrument at the Sealy Center For Structural Biology, UTMB-G (Galveston, TX, USA) equipped with a Kratky-2D Rigaku BioSAXS-1000 detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.15418 nm (I(s) vs s, where s = 4πsin θ/λ and 2θ is the scattering angle). Solute concentrations ranging between 1 and 4 mg/ml were measured at 10°C. SAXS data were acquired from 5 successive 1800 second frames. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled for protein concentration to generate the data displayed for this entry.
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