| MWexperimental | 33 | kDa |
| MWexpected | 36 | kDa |
| VPorod | 48 | nm3 |
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log I(s)
6.75×10-2
6.75×10-3
6.75×10-4
6.75×10-5
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s, nm-1
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Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip
Dunce J, Salmon L, Davies O, Communications Biology 5(1) (2022) DOISASDNR5 – Meiosis protein TEX12 (Testis-expressed protein 12) – F102A, F109E, V116A mutant
Testis-expressed protein 12 (F102A, F109E, V116A)|
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Fits and models
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Synchrotron SAXS data from solutions of the meiosis protein TEX12 (α-helical core, triple mutant) in 20 mM Tris, 150 mM KCl, pH 8 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.095 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 100.00 μl sample at 25 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column. 20 successive 3 second frames were collected through the sample elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Cell temperature = UNKNOWN. Storage temperature = UNKNOWN |
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