Protective Dps-DNA co-crystallization in stressed cells: an in vitro structural study by small-angle X-ray scattering and cryo-electron tomography.

Dadinova LA, Chesnokov YM, Kamyshinsky RA, Orlov IA, Petoukhov MV, Mozhaev AA, Soshinskaya EY, Lazarev VN, Manuvera VA, Orekhov AS, Vasiliev AL, Shtykova EV, FEBS Lett 593(12):1360-1371 (2019) Europe PMC

SASDKD4 – In vitro DNA protection during starvation protein (Dps)/DNA co-crystallization

DNA protection during starvation protein
MWexperimental 19 kDa
MWexpected 224 kDa
log I(s) 1.37×100 1.37×10-1 1.37×10-2 1.37×10-3
DNA protection during starvation protein small angle scattering data  s, nm-1
(sRg)2I(s)/I(0)
DNA protection during starvation protein Kratky plot 1.104 0 3 sRg

Data validation


There are no models related to this curve.

Synchrotron SAXS data from Dps-DNA co-crystalls, in cellulo, were collected on the EMBL-P12 BioSAXS beamline at the PETRAIII storage ring (DESY, Hamburg, Germany) equipped with a robotic sample changer and a 2D photon counting pixel X-ray detector (Pilatus 6M). The scattering intensity I(s) was recorded in the range of the momentum transfer 0.02 < s < 6.0 nm-1, where s = 4πsinθ/λ, and 2θ is the scattering angle, λ= 0.124 nm is the X-ray wavelength. The measurements were carried out in 50 mM Tris-HCl, pH 8, 50 mM NaCl, 0.5 mM EDTA buffer. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

NOTE: Data validation metrics do not apply for this entry (Rg, I(0), MW, etc). The quoted 'experimental MW' is that of the dodecameric protein calculated from the amino acid sequence. The monomer MW is quoted at 19 kDa.

DNA protection during starvation protein (Dps)
Mol. type   Protein
Organism   Escherichia coli (strain K12)
Olig. state   Dodecamer
Mon. MW   18.7 kDa
 
UniProt   P0ABT2
Sequence   FASTA