| MWexperimental | 29 | kDa |
| MWexpected | 28 | kDa |
| VPorod | 47 | nm3 |
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log I(s)
6.53×10-2
6.53×10-3
6.53×10-4
6.53×10-5
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s, nm-1
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Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions.
Delalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E, J Biol Chem 293(18):6637-6646 (2018) Europe PMCSASDB83 – Human dystrophin central domain repeats 16 to 17
Dystrophin central domain repeats 16 to 17.|
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Fits and models
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Synchrotron SAXS data were measured from solutions of Human Dystrophin central domain repeats 16 to 17 (amino acids 1984-2216) in 20 mM Tris 150 mM NaCl, 1 mM EDTA, 2% glycerol buffer using size exclusion chromatography (SEC-SAXS) on the SWING beam line (SOLEIL, Saint-Aubin, France). The sample load concentration was 18.8 mg/mL. The scattering data, I(s) vs s (s = 4π sin θ/λ, where 2θ is the scattering angle) were collected through the corresponding SEC protein elution peak (20 x 1.5 s frames) as well as from the SEC column running buffer. The buffer scattering contributions were subtracted from each sample frame, which were then scaled and averaged to produce the SAXS profile displayed in this entry. The molecular weight estimate (MW) are derived from the Porod volume, Vp, where MW is approximately Vp/1.6. The SEC Rg and I(0) trace is included in the additional files to this entry.
Cell temperature = UNKNOWN. Concentration = UNKNOWN |
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