Evaluating Anti-CD32b F(ab) Conformation Using Molecular Dynamics and Small-Angle X-Ray Scattering.

Sutton EJ, Bradshaw RT, Orr CM, Frendéus B, Larsson G, Teige I, Cragg MS, Tews I, Essex JW, Biophys J 115(2):289-299 (2018) Europe PMC

SASDDP6 – Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment (6G08 F(ab))

Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment
MWI(0) 44 kDa
MWexpected 46 kDa
VPorod 68 nm3
log I(s) 4.43×101 4.43×100 4.43×10-1 4.43×10-2
Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment small angle scattering data  s, nm-1
ln I(s)
Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment Guinier plot ln 4.44×101 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment Kratky plot 1.104 0 √3 sRg
p(r)
Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment pair distance distribution function Rg: 2.5 nm 0 Dmax: 7.3 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment (6G08 F(ab)) in 50mM HEPES, 150mM KCl, pH 7.5, were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.099 nm (l(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 sample concentrations were merged with the highest concentration high angle data to yield the final composite scattering curve.

Sample concentration series: 1.25mg/ml, 2.5mg/ml and 5mg/ml.

Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment (6G08 F(ab))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   45.9 kDa
Sequence   FASTA