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