| MWexperimental | 66 | kDa |
| MWexpected | 77 | kDa |
| VPorod | 107 | nm3 |
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log I(s)
8.13×101
8.13×100
8.13×10-1
8.13×10-2
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s, nm-1
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Conformational heterogeneity of the BTK PHTH domain drives multiple regulatory states.
Lin DY, Kueffer LE, Juneja P, Wales TE, Engen JR, Andreotti AH, Elife 12 (2024) Europe PMCSASDRC9 – Bruton's Tyrosine Kinase - full-length with A384P, S386P, T387P, A388P and L390F mutations
Tyrosine-protein kinase BTK (A384P, S386P, T387P, A388P, L390F)|
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Fits and models
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Synchrotron SAXS data from solutions of mutant Bruton's tyrosine kinase in 20 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 2% v/v glycerol, pH 8 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS, Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 10 mg/ml were measured at 20.9°C. 50 successive 0.200 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
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