| MWexperimental | 233 | kDa |
| MWexpected | 244 | kDa |
| VPorod | 406 | nm3 |
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log I(s)
6.55×10-2
6.55×10-3
6.55×10-4
6.55×10-5
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s, nm-1
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Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes.
Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R, Biochem J (2019) Europe PMCSASDEL9 – Escherichia coli aerobic fatty acid beta-oxidation trifunctional enzyme complex
Fatty acid oxidation complex subunit alphaFatty acid oxidation complex subunit alpha
3-ketoacyl-CoA thiolase FadA (beta subunit)
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Fits and models
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Synchrotron SAXS data from solutions of the E. coli aerobic fatty acid beta-oxidation trifunctional enzyme complex in 20 mM HEPES, 120 mM KCl, 2.5 mM DTT, pH 7.2 were measured at 20°C using size-exclusion chromatography SAXS (SEC-SAXS) on the B21 beam line at the Diamond Light Source (Oxfordshire, UK) using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). The data were collected as 540 successive 3 second frames through the SEC elution profile (sample concentration = 6.20 mg/ml ). The SAXS data were measured from the sample and buffer from a Shodex KW403 column at flow rate of 0.16 mL/min. The sample-peak data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the individual subtracted data sets were scaled and averaged to generate the scattering profile displayed in this entry.
SEC column = UNKNOWN. Sample injection volume = UNKNOWN. Flow rate = UNKNOWN |
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