| MWexperimental | 243 | kDa |
| MWexpected | 270 | kDa |
| VPorod | 439 | nm3 |
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log I(s)
1.56×103
1.56×102
1.56×101
1.56×100
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s, nm-1
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Controlled modulation of the dynamics of the Deinococcus grandis Dps N-terminal tails by divalent metals.
Guerra JPL, Blanchet CE, Vieira BJC, Waerenborgh JC, Jones NC, Hoffmann SV, Pereira AS, Tavares P, Protein Sci :e4567 (2023) Europe PMCSASDQW4 – DNA-binding protein from starved cells: DgrDpsWT + 24 Zn2+ in 50 mM MOPS pH 7.0, 230 mM NaCl
DNA protection during starvation, DPS (Ferritin superfamily)|
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Fits and models
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Synchrotron SAXS data from solutions of DgrDpsWT + 24 Zn2+ in 50 mM MOPS pH 7.0, 230 mM NaCl were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 6 m and at a wavelength of λ = 0.124 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 GE Superdex 200 Increase 5/150 column at 25°C. 15 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.
Both the CORAL and CRYSOL model fits of the same DgrDpsWT atomistic/rigid-body model are displayed consecutively (middle and bottom). The gene sequence used in this project was NCBI Reference Sequence: WP_058978256.1, which lacks the initial 10 amino acids of UniProt sequence A0A100HLL5. https://www.ncbi.nlm.nih.gov/protein/WP_058978256.1 |
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