| MWexperimental | 41 | kDa |
| MWexpected | 39 | kDa |
| VPorod | 70 | nm3 |
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log I(s)
3.68×10-2
3.68×10-3
3.68×10-4
3.68×10-5
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s, nm-1
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Structural and biochemical analysis of Escherichia coli ObgE, a central regulator of bacterial persistence.
Gkekas S, Singh RK, Shkumatov AV, Messens J, Fauvart M, Verstraeten N, Michiels J, Versées W, J Biol Chem 292(14):5871-5883 (2017) Europe PMCSASDBU6 – Apo form of the C-terminal deletion mutant of ObgE from E.coli (ObgE_340)
GTPase ObgE/CgtA|
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Fits and models
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Rg, nm
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Synchrotron SAXS data from solutions of the Apo form of the C-terminal deletion mutant of ObgE from E.coli (ObgE_340) in 20 mM HEPES, 300 mM NaCl, 250 mM imidazole, 5 mM MgCl2, 2 mM DTT, pH 7.5 were collected at the SWING beam line at the SOLEIL Synchrotron (Saint-Aubin, France) using a CCD AVIEX detector at a sample-detector distance of 2.0 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). Data collection was performed at at 10°C. 255 successive 2.8 second frames were collected through an HPLC-SEC elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled for protein concentration, then averaged to produce the final SAXS profile displayed in this entry.
The sample protein includes an N-terminal poly-histidine tag; frames corresponding to the peak in HPLC-SAXS run were averaged using DATAVER v0.2 (r3709) |
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