| MWI(0) | 29 | kDa |
| MWexpected | 30 | kDa |
| VPorod | 41 | nm3 |
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log I(s)
4.95×103
4.95×102
4.95×101
4.95×100
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s, nm-1
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Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the adenylate cyclase toxin.
Espinosa-Vinals CA, Masin J, Holubova J, Stanek O, Jurnecka D, Osicka R, Sebo P, Bumba L, J Biol Chem :100833 (2021) Europe PMCSASDL62 – The truncated RTX domain of adenylate cyclase toxin CyaA - construct RTX-1 (amino acids 1132-1294 and 1562-1681 of CyaA)
hybrid RTX-1 construct (amino acids 1132-1294 and 1562-1681 of CyaA)|
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Fits and models
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Synchrotron SAXS data from solutions of RTX-1 in 10 mM Tris HCl, 150 mM NaCl, 10 mM CaCl₂, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm. Solute concentrations ranging between 1 and 8 mg/ml were measured at 10°C. 20 successive 0.050 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 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.
The model displayed is a bead-occupancy and volume-corrected spatial representation derived from an aligned individual model cohort (damfilt) and does not correspond to the fit to the SAXS data displayed in this entry. |
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