Antibody binding geometry and affinity control inhibitory hFcγRIIB receptor signaling.

Fisher H Sutton EJ, Oldham RJ, Bradshaw RT, Duriez PJ, Frendéus B, Larsson G, Manfredi G, Martin-Fernandez ML, Mockridge I, Needham SR, Rolfe DJ, Orr CM, Patel K, Roghanian A, Simpson A, Tully MD, Teige I, Tornberg UC, Tynan CJ, Pendower A, Kim J, Tennenhouse A, Fleishman SJ, Essex JW, Tews I, Cragg MS, Immunity (2026) Europe PMC

SASDU97 – Human IgG1 F(ab') 6C11

Human IgG1 F(ab') 6C11
MWexperimental 33 kDa
MWexpected 24 kDa
VPorod 56 nm3
log I(s) 4.93×100 4.93×10-1 4.93×10-2 4.93×10-3
Human IgG1 F(ab') 6C11 small angle scattering data  s, nm-1
ln I(s)
Human IgG1 F(ab') 6C11 Guinier plot ln 4.94×100 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Human IgG1 F(ab') 6C11 Kratky plot 1.104 0 3 sRg
Dmax: 7.6 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Human IgG1 F(ab') 6C11 in 50 mM HEPES, 150 mM KCl, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.3 and 5 mg/ml were measured at 20°C. 10 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Human IgG1 F(ab') 6C11
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   24.2 kDa
Sequence   FASTA