| MWexperimental | 349 | kDa |
| MWexpected | 87 | kDa |
| VPorod | 617 | nm3 |
|
log I(s)
2.08×10-1
2.08×10-2
2.08×10-3
2.08×10-4
|
s, nm-1
|
The mechanism behind acetyl-CoA-mediated activation in Mycobacterium tuberculosis isocitrate lyase 2 and the contribution of its unique protein features to allostery and selectivity
Ashish Sethi.SASDVP7 – Mycobacterium tuberculosis Isocitrate Lyase 2 mutant (E640C, N731C, E733C)
Isocitrate lyase 2 (E640C, N731C, E733C)|
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Fits and models
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Synchrotron SAXS data from solutions of Mycobacterium tuberculosis Isocitrate Lyase 2 mutant (E640C, N731C, E733C) in 50 mM HEPES, 150 mM NaCl, pH 7.5 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.10332 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) co-flow SAXS was employed. The SEC parameters were as follows: A 50.00 μl sample at 5 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 300 successive 1 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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