| MWexperimental | 126 | kDa |
| MWexpected | 62 | kDa |
| VPorod | 186 | nm3 |
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log I(s)
5.17×10-3
5.17×10-4
5.17×10-5
5.17×10-6
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s, nm-1
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Conformational flexibility of EptA driven by an interdomain helix provides insights for enzyme-substrate recognition.
Anandan A, Dunstan NW, Ryan TM, Mertens HDT, Lim KYL, Evans GL, Kahler CM, Vrielink A, IUCrJ 8(Pt 5):732-746 (2021) Europe PMCSASDK28 – Lipid A phosphoethanolamine transferase in n-dodecyl-phosphocholine micelles
YhbX/YhjW/YijP/YjdB family protein (L152F)|
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Fits and models
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Rg, nm
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Synchrotron SAXS data from solutions of Lipid A phosphoethanolamine transferase in 50 mM HEPES, 100 mM NaCl, 0.14% Fos-Choline 12 (FC-12), pH 7 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.103 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 7 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Number of frames = UNKNOWN |
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