| MWexperimental | 14 | kDa |
| MWexpected | 17 | kDa |
| VPorod | 30 | nm3 |
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log I(s)
1.70×103
1.70×102
1.70×101
1.70×100
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s, nm-1
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A new protein-dependent riboswitch activates ribosomal frameshifting
Betts J, Jeffries C, Passchier T, Kung H, Graham S, Abdelhamid M, Howard J, Craggs T, Graham S, Brierley I, Leake M, Quinn S, Hill C, (2025) DOISASDWQ5 – 2A protein from Theiler's murine encephalomyelitis virus (TMEV)
Genome polyprotein|
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Fits and models
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Synchrotron SAXS data from solutions of 2A protein in 20 mM HEPES pH 7.4, 1 M KCl, 2% v/v glycerol, 1 mM DTT, were collected on the EMBL P12 beam line at PETRA III (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 50.00-100 μl sample at 4.0 mg/ml were injected at a 0.35 ml/min flow rate onto a GE Superdex 75 Increase 5/150 column at 20°C. 143 successive 0.250 second frames were collected through two consecutive SEC-SAXS runs, spanning the sample elution peaks of the protein. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
The data displayed in this entry show the averaged scattering intensity derived from of two independent SEC-SAXS measurements (a 50 µl and 100 µl injection, respectively). The full entry archive contains the unsubtracted 1D-data frames spanning both individual SEC-SAXS runs, in addition to the respective processed SEC-SAXS data for each run, prior to scaling and averaging. Additional CORAL, MONSA, GASBOR and DAMMIN models are also made available in the full entry zip archive. |
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