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 Oct 23)

PMID: 19683001 doi: 10.1016/j.jmb.2009.08.005

Published in SASBDB: 2015 Jul 7

SASDA55 – Nucleoplasmin Sample: Nucleoplasmin pentamer, 110 kDa Escherichia coli protein Buffer: 20 mM Pipes buffer 150 mM NaCl, pH: 7.5 Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Dec 3 RgGuinier 4.0 nm Dmax 12.6 nm VolumePorod 210 nm3

SASDA65 – Nucleoplasmin-H5 complex Sample: NP-H5 pentamer, 200 kDa Escherichia coli protein Buffer: 20 mM Pipes buffer 150 mM NaCl, pH: 7.5 Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Dec 3 RgGuinier 5.2 nm Dmax 16.7 nm VolumePorod 410 nm3

SASDA75 – Nucleoplasmin-H2AH2B complex Sample: NP-H2AH2B pentamer, 250 kDa Escherichia coli protein Buffer: 20 mM Pipes buffer 150 mM NaCl, pH: 7.5 Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2014 Dec 3 RgGuinier 4.7 nm Dmax 14.5 nm VolumePorod 470 nm3