| MWexperimental | 47 | kDa |
| MWexpected | 47 | kDa |
| VPorod | 66 | nm3 |
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log I(s)
2.34×102
2.34×101
2.34×100
2.34×10-1
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s, nm-1
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Structural basis underlying the synergism of NADase and SLO during group A Streptococcus infection.
Tsai WJ, Lai YH, Shi YA, Hammel M, Duff AP, Whitten AE, Wilde KL, Wu CM, Knott R, Jeng US, Kang CY, Hsu CY, Wu JL, Tsai PJ, Chiang-Ni C, Wu JJ, Lin YS, Liu CC, Senda T, Wang S, Commun Biol 6(1):124 (2023) Europe PMCSASDM47 – NAD glycohydrolase (NADase)
NAD glycohydrolase|
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Fits and models
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Synchrotron SAXS data from solutions of NADase in phosphate buffered saline, pH 7.4 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 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 10 mg/ml was injected at a 0.50 ml/min flow rate onto a Shodex KW-800 series column at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted from those sample frames encompassing the SEC elution peak.
The multistate model of NADase is composed of a 40% volume fraction of compact and a 60% volume fraction of extended states, respectively. |
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