The Conformation of the N-Terminal Tails of Deinococcus grandis Dps Is Modulated by the Ionic Strength

Guerra J, Blanchet C, Vieira B, Almeida A, Waerenborgh J, Jones N, Hoffmann S, Tavares P, Pereira A, International Journal of Molecular Sciences 23(9):4871 (2022) DOI

SASDN38 – DNA-binding protein from starved cells: DgrDpsWT in 50 mM MOPS, 480 mM NaCl pH 7.0

DNA protection during starvation, DPS (Ferritin superfamily)
MWexperimental 318 kDa
MWexpected 270 kDa
VPorod 430 nm3
log I(s) 1.67×10-1 1.67×10-2 1.67×10-3 1.67×10-4
DNA protection during starvation, DPS (Ferritin superfamily) small angle scattering data  s, nm-1
ln I(s)
DNA protection during starvation, DPS (Ferritin superfamily) Guinier plot ln 1.67×10-1 Rg: 4.8 nm 0 (4.8 nm)-2 s2
(sRg)2I(s)/I(0)
DNA protection during starvation, DPS (Ferritin superfamily) Kratky plot 1.104 0 3 sRg
p(r)
DNA protection during starvation, DPS (Ferritin superfamily) pair distance distribution function Rg: 4.9 nm 0 Dmax: 20.5 nm

Data validation


Fits and models


log I(s)
 s, nm-1
DNA protection during starvation, DPS (Ferritin superfamily) GASBOR model

Synchrotron SAXS data from solutions of DgrDpsWT in 50 mM MOPS-NaOH, 480 mM NaCl, pH 7 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 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 15°C. 40 successive 0.100 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.

DNA protection during starvation, DPS (Ferritin superfamily) (DgrDpsWT)
Mol. type   Protein
Organism   Deinococcus grandis
Olig. state   Dodecamer
Mon. MW   22.5 kDa
 
UniProt   A0A100HLL5 (10-214)
Sequence   FASTA