| MWexperimental | 391 | kDa |
| MWexpected | 367 | kDa |
| VPorod | 557 | nm3 |
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log I(s)
1.74×10-1
1.74×10-2
1.74×10-3
1.74×10-4
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s, nm-1
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Activity of lymphostatin, a lymphocyte inhibitory virulence factor of pathogenic Escherichia coli, is dependent on a cysteine protease motif.
Bease AG, Blackburn EA, Chintoan-Uta C, Webb S, Cassady-Cain RL, Stevens MP, J Mol Biol :167200 (2021) Europe PMCSASDKN9 – Lymphostatin C1480A mutant pH 7.5
Efa1/LifA protein (C1480A mutant)|
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Fits and models
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Synchrotron SAXS data of C1480A single point mutation Lymphostatin in 50 mM Bis-Tris, pH 7.5; 100 mM NaCl; 3% glycerol (v/v) were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector 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 using a 2.4 mL superdex200 3.2/300 chromatography column (GE healthcare). 35 μl of mutant lymphostatin solution at 1.93 mg/ml was injected at 0.075 ml/min and 620 successive 1.5 second data-frames were collected at 15°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the eluted buffer with no macromolecular component was subtracted.
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