| MWI(0) | 52 | kDa |
| MWexpected | 60 | kDa |
| VPorod | 144 | nm3 |
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log I(s)
2.72×10-1
2.72×10-2
2.72×10-3
2.72×10-4
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s, nm-1
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How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.
Mias-Lucquin D, Dos Santos Morais R Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O, J Struct Biol :107411 (2019) Europe PMCSASDFU4 – Conformation of R11-15 human dystrophin fragment in interaction with zwitterionic phospholipid bicelles (SANS)
Dystrophin (R11-15 human dystrophin fragment)|
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Fits and models
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SANS data from solutions of the R11-15 human dystrophin fragment with zwitterionic phospholipid bicelles in 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH 7.1 were collected on the D22 beam line at the ILL (Grenoble, France) using a 3He multidetector 128 linear sensitive Reuter-Stokes detector at a wavelength of λ = 0.6 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.60 mg/ml was measured at 22°C. One 1200 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Data were collected at two sample detector positions: 1) 1.4 m for 5 min using a neutron wavelength of 0.6 nm and; 2) 8 m for 20 min using a neutron wavelength of 0.6 nm. Both datasets were recorded on the same sample at 5.6 mg/mL, measured at 22 °C.
Tags:
sans
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