| MWexperimental | 243 | kDa |
| MWexpected | 258 | kDa |
| VPorod | 363 | nm3 |
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log I(s)
1.16×10-2
1.16×10-3
1.16×10-4
1.16×10-5
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s, nm-1
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Structural insights into the enzymatic breakdown of azomycin-derived antibiotics by 2-nitroimdazole hydrolase (NnhA).
Ahmed FH, Liu JW, Royan S, Warden AC, Esquirol L, Pandey G, Newman J, Scott C, Peat TS, Commun Biol 7(1):1676 (2024) Europe PMCSASDVG6 – 2-nitroimidazole nitrohydrolase
2-nitroimidazole nitrohydrolase (T2I, G14D, K73R)|
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Fits and models
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Synchrotron SAXS data from solutions of 2-nitroimidazole nitrohydrolase in 25 mM Tris-HCl, 150 mM NaCl, 5% (v/v) glycerol, pH 7.6 were collected on the BioSAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 2M detector at a sample-detector distance of 3.2 m and at a wavelength of λ = 0.1 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 3.5 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 5/150 column at 25°C. 29 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.
The molecular weight estimate (243 kDa) was calculated from Bayesian Inference (84.5% probability) in the molecular weight range credibility interval spanning 221.1 kDa to 372.7 kDa (98.7% probability). |
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