| MWI(0) | 110 | kDa |
| MWexpected | 127 | kDa |
| VPorod | 168 | nm3 |
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log I(s)
2.18×104
2.18×103
2.18×102
2.18×101
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s, nm-1
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Structural Basis for Antigen Recognition by Transglutaminase 2-specific Autoantibodies in Celiac Disease.
Chen X, Hnida K, Graewert MA, Andersen JT, Iversen R, Tuukkanen A, Svergun D, Sollid LM, J Biol Chem 290(35):21365-75 (2015) Europe PMCSASDA48 – transglutaminase2:anti-transglutaminase2 FAB1 antibody complex
anti-TG2 antibody (679 14 E06)transglutaminase 2
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Fits and models
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Synchrotron SAXS
data from solutions of
transglutaminase2:anti-transglutaminase2 FAB1 antibody complex
in
20 mM Tris 150mM NaCl 1mM EDTA, pH 7.2
were collected
on the
EMBL P12 beam line
at the PETRA III storage ring
(DESY; Hamburg, Germany)
using a Pilatus 2M detector
at a sample-detector distance of 3.1 m and
at a wavelength of λ = 0.12 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 9.00 mg/ml was measured
at 10°C.
20 successive
0.050 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.
Structural basis for antigen recognition by transglutaminase 2-specific autoantibodies in celiac disease. SAXS profile of the complex formed between transglutaminase2 bound to anti-transglutaminase2 antibody (679 14 E06) FAB1. |
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