A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models.

Taneva SG, Bañuelos S, Falces J, Arregi I, Muga A, Konarev PV, Svergun DI, Velázquez-Campoy A, Urbaneja MA, J Mol Biol 393(2):448-63 (2009) Europe PMC

SASDA65 – Nucleoplasmin-H5 complex

NP-H5
MWexperimental 200 kDa
MWexpected 200 kDa
VPorod 410 nm3
log I(s) 4.74×10-1 4.74×10-2 4.74×10-3 4.74×10-4
NP-H5 small angle scattering data  s, nm-1
ln I(s)
NP-H5 Guinier plot ln 4.74×10-1 Rg: 5.2 nm 0 (5.2 nm)-2 s2
(sRg)2I(s)/I(0)
NP-H5 Kratky plot 1.104 0 3 sRg
Dmax: 16.7 nm

Data validation


Fits and models


log I(s)
 s, nm-1
NP-H5 MONSA model

Synchrotron SAXS data from solutions of Nucleoplasmin-H5 complex in 20 mM Pipes buffer 150 mM NaCl, pH 7.5 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 3 and 5 mg/ml were measured at 10°C. Four successive 15 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.

Tags: X33
NP-H5 (NP-H5)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Pentamer
Mon. MW   40 kDa