| MWexperimental | 78 | kDa |
| MWexpected | 80 | kDa |
| VPorod | 96 | nm3 |
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log I(s)
2.76×101
2.76×100
2.76×10-1
2.76×10-2
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s, nm-1
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Solution Structure of SpoIVB Reveals Mechanism of PDZ Domain-Regulated Protease Activity.
Xie X, Guo N, Xue G, Xie D, Yuan C, Harrison J, Li J, Jiang L, Huang M, Front Microbiol 10:1232 (2019) Europe PMCSASDFJ3 – Maltose binding protein-SpoIVB peptidase fusion (MBP-SpoIVB)
SpoIVB peptidase (MBP fusion)|
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Fits and models
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Synchrotron SAXS data from solutions of MBP-SpoIVB peptidase fusion protein in 20 mM Tris-HCl, 150 mM NaCl, 5% glycerol, pH 8 were collected on the BL19U2 beam line at the Shanghai Synchrotron Radiation Facility (SSRF, Shanghai, China) using a Pilatus 1M detector at a sample-detector distance of 2.3 m and at a wavelength of λ = 0.103 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 10°C. 20 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 originally deposited p(r) profile is included in the full entry zip archive. |
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