| MWI(0) | 65 | kDa |
| MWexpected | 82 | kDa |
| VPorod | 165 | nm3 |
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log I(s)
1.72×102
1.72×101
1.72×100
1.72×10-1
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s, nm-1
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Structural Insights of Shigella Translocator IpaB and Its Chaperone IpgC in Solution
Ferrari M, Charova S, Sansonetti P, Mylonas E, Gazi A, Frontiers in Cellular and Infection Microbiology 11 (2021) DOISASDKR9 – The chaperone protein IpgC/invasin IpaB heterodimer complex from Shigella flexneri
T3SS Chaperone protein IpgCInvasin IpaB
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Fits and models
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Synchrotron SAXS data from solutions of the IpgC/IpaB heterodimer complex in 20 mM HEPES, 100 mM NaCl, pH 7.4 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.09199 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.6 and 5.5 mg/ml were measured at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
Storage temperature = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN |
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