| MWexperimental | 257 | kDa |
| MWexpected | 276 | kDa |
| VPorod | 437 | nm3 |
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log I(s)
5.07×101
5.07×100
5.07×10-1
5.07×10-2
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s, nm-1
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SAXS Structural Studies of Dps from Deinococcus radiodurans Highlights the Conformation of the Mobile N-Terminal Extensions.
Santos SP, Cuypers MG, Round A, Finet S, Narayanan T, Mitchell EP, Romão CV, J Mol Biol 429(5):667-687 (2017) Europe PMCSASDBG7 – Dps1, DNA binding protein under starvation conditions (SEC-SAXS)
DNA protection during starvation protein 1|
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Fits and models
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Synchrotron SAXS data, I(s) vs s (s = 4π sin θ/λ, where 2θ is the scattering angle) were collected from a sample of Dps1, (DNA binding protein under starvation conditions) using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS) at the BM29 beam line on the ESRF storage ring (Grenoble, France). Data (1500 successive 1 second frames), were collected using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.09919 nm. The SEC mobile phase consisted of 20 mM Tris-HCl, 150 mM NaCl, pH 7.5, (20°C) with a sample injection concentration of 10 mg/ml. Data obtained from solute-free eluates and SEC-elution peak were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted from the SEC-peak frames to produce the data displayed in this entry.
SEC column = UNKNOWN. Sample injection volume = UNKNOWN. Flow rate = UNKNOWN |
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