pH Sensitivity of the SERF1a Conformational Ensemble

Huang S, Shih O, Jeng U, Chang C, Lin J, Malliavin T, ACS Omega (2026) DOI

SASDWY9 – Small EDRK-rich factor 1 protein (SERF1a) at pH 6

Isoform Short of Small EDRK-rich factor 1
MWI(0) 52 kDa
MWexpected 7 kDa
VPorod 10 nm3
log I(s) 3.74×10-2 3.74×10-3 3.74×10-4 3.74×10-5
Isoform Short of Small EDRK-rich factor 1 small angle scattering data  s, nm-1
ln I(s)
Isoform Short of Small EDRK-rich factor 1 Guinier plot ln 3.75×10-2 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Isoform Short of Small EDRK-rich factor 1 Kratky plot 1.104 0 √3 sRg
p(r)
Isoform Short of Small EDRK-rich factor 1 pair distance distribution function Rg: 2.6 nm 0 Dmax: 10.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Isoform Short of Small EDRK-rich factor 1 OTHER model
log I(s)
 s, nm-1
Isoform Short of Small EDRK-rich factor 1 OTHER model
log I(s)
 s, nm-1
Isoform Short of Small EDRK-rich factor 1 OTHER model
Synchrotron SAXS data from solutions of SERF1a in 20 mM sodium phosphate, 20 mM NaCl, pH 6 were collected on the 13A beam line at the Taiwan Photon Source, NSRRC (Hsinchu, Taiwan) using a Eiger X 9M detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.08266 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 15 and 15 mg/ml were measured at 10°C. Five 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Isoform Short of Small EDRK-rich factor 1 (SERF1a)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   7.3 kDa
 
UniProt   O75920-2 (1-62)
Sequence   FASTA