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

SASDDG2 – Glycosylated Human Immunoglobulin G Fc Region

Glycosylated human immunoglobulin G Fc region
MWI(0) 54 kDa
MWexpected 53 kDa
VPorod 66 nm3
log I(s) 3.90×10-2 3.90×10-3 3.90×10-4 3.90×10-5
Glycosylated human immunoglobulin G Fc region small angle scattering data  s, nm-1
ln I(s)
Glycosylated human immunoglobulin G Fc region Guinier plot ln 3.90×10-2 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Glycosylated human immunoglobulin G Fc region Kratky plot 1.104 0 √3 sRg
p(r)
Glycosylated human immunoglobulin G Fc region pair distance distribution function Rg: 2.8 nm 0 Dmax: 10.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Glycosylated human immunoglobulin G Fc region MODELLER model
Synchrotron SAXS data from solutions of glycosylated 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 3.25 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

Glycosylated human immunoglobulin G Fc region (gFc)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   24.9 kDa
 
UniProt   P01857 (108-329)
Sequence   FASTA
 
PDB ID   1HZH