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 Dec 4)
PMID: 30513259
doi: 10.1080/19420862.2018.1546086 		Submitted to SASBDB: 2018 Dec 8
Published in SASBDB:

SASDDG2 – Glycosylated Human Immunoglobulin G Fc Region

Glycosylated human immunoglobulin G Fc region experimental SAS data
MODELLER model
Sample: Glycosylated human immunoglobulin G Fc region dimer, 53 kDa Homo sapiens protein
Buffer: 20 mM Citrate-Phosphate, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Mar 5
RgGuinier 2.7 nm
Dmax 10.2 nm
VolumePorod 66 nm3

SASDDH2 – Aglycosylated Human Immunoglobulin G Fc Region

Aglycosylated human immunoglobulin G Fc region experimental SAS data
MODELLER model
Sample: Aglycosylated human immunoglobulin G Fc region dimer, 51 kDa Homo sapiens protein
Buffer: 20 mM Citrate-Phosphate, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Mar 5
RgGuinier 2.9 nm
Dmax 9.8 nm
VolumePorod 60 nm3