| MWexperimental | 50 | kDa |
| MWexpected | 50 | kDa |
| VPorod | 85 | nm3 |
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log I(s)
2.20×10-2
2.20×10-3
2.20×10-4
2.20×10-5
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s, nm-1
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Insights into the stereochemical mechanism of the B(12)-dependent radical SAM glutamine C- methyltransferase (QCMT).
Bourdin T, Guillot A, Mauger M, Lefranc B, Gervason S, Glousieau M, Grimaldi S, Leprince J, Thureau A, Benjdia A, Berteau O, Commun Biol (2026) Europe PMCSASDVY7 – Glutamine C‐methyltransferase without cobalamin from Methanoculleus thermophilus
B12-binding domain/radical SAM domain protein, MJ_0865 family|
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Fits and models
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Synchrotron SAXS data from solutions of glutamine C‐methyltransferase without cobalamin in 50 mM Tris, 300 mM NaCl, 5% glycerol, pH 8 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1033 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 μl sample at 5 mg/ml was injected at a 0.25 ml/min flow rate onto a Cytiva Superdex 200 5/150 column at 20°C. 646 successive 0.990 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.
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