Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling.

Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M, Nat Commun 11(1):2905 (2020) Europe PMC

SASDFQ6 – DNA-binding protein HU-alpha, E34K

DNA-binding protein HU-alpha, E34K
MWexperimental 20 kDa
MWexpected 19 kDa
VPorod 36 nm3
log I(s) 4.49×102 4.49×101 4.49×100 4.49×10-1
DNA-binding protein HU-alpha, E34K small angle scattering data  s, nm-1
ln I(s)
DNA-binding protein HU-alpha, E34K Guinier plot ln 4.49×102 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
DNA-binding protein HU-alpha, E34K Kratky plot 1.104 0 √3 sRg
p(r)
DNA-binding protein HU-alpha, E34K pair distance distribution function Rg: 2.2 nm 0 Dmax: 6.7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
DNA-binding protein HU-alpha, E34K CHIMERA model
Synchrotron SAXS data from solutions of DNA-binding protein HU-alpha, E34K in 10 mM Bis-Tris, 100 mM NaCl, pH 7.5 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). at 10°C. 300 successive 3 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.

Storage temperature = UNKNOWN. Concentration = UNKNOWN

DNA-binding protein HU-alpha, E34K
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Dimer
Mon. MW   9.5 kDa
 
UniProt   P0ACF0 (1-90)
Sequence   FASTA