Conformational Plasticity of the Immunoglobulin Fc Domain in Solution.

Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M, Structure 26(7):1007-1014.e2 (2018) PubMed

SASDDT4 – Fc region of Immunoglobulin G1 (IgG1 Fc)

Immunoglobulin heavy constant gamma 1
MWexperimental 51 kDa
MWexpected 53 kDa
VPorod 70 nm3
log I(s) 4.14×102 4.14×101 4.14×100 4.14×10-1
Immunoglobulin heavy constant gamma 1 small angle scattering data  s, nm-1
ln I(s)
Immunoglobulin heavy constant gamma 1 Guinier plot ln 4.14×102 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Immunoglobulin heavy constant gamma 1 Kratky plot 1.104 0 3 sRg
p(r)
Immunoglobulin heavy constant gamma 1 pair distance distribution function Rg: 2.7 nm 0 Dmax: 10 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Immunoglobulin heavy constant gamma 1 BILBOMD model

Synchrotron SAXS data from solutions of the Fc region of Immunoglobulin G1 (IgG1 Fc) in 20mM HEPES, 50mM NaCl, pH 7.5, were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.103 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 14 mg/ml were measured at 20°C. 33 successive 0.300 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Immunoglobulin heavy constant gamma 1 (IgG1 Fc)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   26.4 kDa
 
UniProt   P01857
Sequence   FASTA