Characterisation of Entamoeba histolytica Anti-Silencing Function 1 as a histone chaperone.

Gandhi S, Vasudevan D, Biochimie (2025) Europe PMC

SASDXB7 – Entamoeba histolytica Anti-Silencing Function 1 (ASF1) with C terminal His6-tag

Anti-Silencing Function 1
MWexperimental 28 kDa
MWexpected 28 kDa
VPorod 40 nm3
log I(s) 2.65×101 2.65×100 2.65×10-1 2.65×10-2
Anti-Silencing Function 1 small angle scattering data  s, nm-1
ln I(s)
Anti-Silencing Function 1 Guinier plot ln 2.66×101 Rg: 3.5 nm 0 (3.5 nm)-2 s2
(sRg)2I(s)/I(0)
Anti-Silencing Function 1 Kratky plot 1.104 0 √3 sRg
p(r)
Anti-Silencing Function 1 pair distance distribution function Rg: 3.4 nm 0 Dmax: 10.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Anti-Silencing Function 1 ALPHAFOLD model
log I(s)
 s, nm-1
Anti-Silencing Function 1 DAMFILT model
log I(s)
 s, nm-1
Anti-Silencing Function 1 DAMMIF model
Synchrotron SAXS data from solutions of Entamoeba histolytica Anti-Silencing Function 1 (ASF1) with C terminal His6-tag in 20 mM Tris, 150 mM NaCl, and 2 mM β-mercaptoethanol, pH 7.5 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.9794 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 20°C. 10 successive 1 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.

Anti-Silencing Function 1 (ASF1)
Mol. type   Protein
Organism   Entamoeba histolytica strain HM-1:IMSS
Olig. state   Monomer
Mon. MW   27.7 kDa
 
UniProt   C4LX08 (1-234)
Sequence   FASTA