| MWexperimental | 91 | kDa |
| MWexpected | 99 | kDa |
| VPorod | 127 | nm3 |
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log I(s)
9.03×101
9.03×100
9.03×10-1
9.03×10-2
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s, nm-1
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Structure-guided disulfide engineering restricts antibody conformation to elicit TNFR agonism.
Elliott IG, Fisher H, Chan HTC, Inzhelevskaya T, Mockridge CI, Penfold CA, Duriez PJ, Orr CM, Herniman J, Müller KTJ, Essex JW, Cragg MS, Tews I, Nat Commun 16(1):3495 (2025) Europe PMCSASDUJ8 – Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain C224S/C225S mutant
Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain C224S/C225SHuman immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - kappa light chain
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Fits and models
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Rg, nm
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Synchrotron SAXS
data from solutions of
Human immunoglobulin gamma 2 (IgG2) ChiLob 7/4 F(ab')2 - heavy chain C224S/C225S mutant
in
50 mM HEPES, 150 mM KCl, pH 7.5
were collected
on the
BM29 beam line
at the ESRF storage ring
(Grenoble, France)
using a Pilatus3 2M 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).
In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 45.00 μl sample
at 4.8 mg/ml was injected at a 0.30 ml/min flow rate
onto a Agilent Bio SEC-3, 300 Å column
at 20°C.
490 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.
Full EOM/GAGOE results are made available in the full entry zip archive. |
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