The sequence–structure–function relationship of intrinsic ERα disorder

Du Z, Wang H, Luo S, Yun Z, Wu C, Yang W, Buck M, Zheng W, Hansen A, Kao H, Yang S, Nature (2025) DOI

SASDVC5 – SEC-SAXS data of phosphorylated estrogen receptor alpha (pSer118), N-terminal domain (NTD) at pH 7.4

Estrogen receptor
MWexperimental 20 kDa
MWexpected 20 kDa
VPorod 70 nm3
log I(s) 3.83×100 3.83×10-1 3.83×10-2 3.83×10-3
Estrogen receptor small angle scattering data  s, nm-1
ln I(s)
Estrogen receptor Guinier plot ln 3.83×100 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Estrogen receptor Kratky plot 1.104 0 3 sRg
Dmax: 16 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the phosphorylated N-terminal domain of estrogen receptor alpha (pSer118) in 20 mM sodium phosphate, 50 mM NaCl, 0.05 mM TCEP, pH 7.4 were collected on the 16-ID (LiX) beam line at the National Synchrotron Light Source II (NSLS-II; Upton, NY, USA) using a Pilatus3 S 1M, Pilatus3 900 K detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.08189 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 100.00 μl sample at 2 mg/ml was injected at a 0.35 ml/min flow rate onto a Cytiva Superdex 75 Increase 5/150 column at 4°C. 360 successive 2 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.

Estrogen receptor (ER-NTD)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   20.2 kDa
 
UniProt   P03372 (1-184)
Sequence   FASTA