CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering.

Yageta S, Imamura H, Shibuya R, Honda S, MAbs (2018) Europe PMC

SASDDH2 – Aglycosylated Human Immunoglobulin G Fc Region

Aglycosylated human immunoglobulin G Fc region
MWI(0) 51 kDa
MWexpected 51 kDa
VPorod 60 nm3
log I(s) 3.60×10-2 3.60×10-3 3.60×10-4 3.60×10-5
Aglycosylated human immunoglobulin G Fc region small angle scattering data  s, nm-1
ln I(s)
Aglycosylated human immunoglobulin G Fc region Guinier plot ln 3.60×10-2 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Aglycosylated human immunoglobulin G Fc region Kratky plot 1.104 0 √3 sRg
p(r)
Aglycosylated human immunoglobulin G Fc region pair distance distribution function Rg: 2.9 nm 0 Dmax: 9.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Aglycosylated human immunoglobulin G Fc region MODELLER model
Synchrotron SAXS data from solutions of aglycosylated Human Immunoglobulin G (Fc Region) in 20 mM Citrate-Phosphate, pH 7 were collected on the BL-10C beam line at the Photon Factory (PF), High Energy Accelerator Research Organization (KEK) storage ring (Tsukuba, Japan) using a Pilatus3 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.12 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.19 mg/ml was measured at 25°C. 15 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.

Storage temperature = UNKNOWN

Aglycosylated human immunoglobulin G Fc region (aFc)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   25.7 kDa
 
UniProt   P01857 (104-330)
Sequence   FASTA
 
PDB ID   1HZH