pH Sensitivity of the SERF1a Conformational Ensemble

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

SASDWZ9 – Small EDRK-rich factor 1 protein (SERF1a) at pH 6.8

Isoform Short of Small EDRK-rich factor 1
MWexperimental 10 kDa
MWexpected 7 kDa
VPorod 11 nm3
log I(s) 1.16×10-2 1.16×10-3 1.16×10-4 1.16×10-5
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 1.16×10-2 Rg: 2.5 nm 0 (2.5 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: 8.8 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 20 mM sodium phosphate, 20 mM NaCl, pH 6.8 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). One solute concentration of 15.00 mg/ml was 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.

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