| MWI(0) | 165 | kDa |
| MWexpected | 144 | kDa |
| VPorod | 225 | nm3 |
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log I(s)
1.00×105
1.00×104
1.00×103
1.00×102
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s, nm-1
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Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes.
Czech A, Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z, Sci Rep 9(1):2465 (2019) Europe PMCSASDDJ5 – Mammalian prion protein mRNA (PrP mRNA wild type) with LiCl
octo-repeat PrP mRNA|
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Fits and models
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Synchrotron SAXS data from solutions of mammalian prion protein mRNA (PrP mRNA wild type) in 10 mM Tris buffer with 100 mM LiCl, pH 7.5, were collected on the EMBL-P12 beam line at the PETRA III storage ring (DESY, Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.5 and 4 mg/ml were measured at 20°C. 20 successive 0.050 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 concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
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