Molecular basis of Fab-dependent IgA antibody recognition by gut-associated metallopeptidases

SASDX65 – IgA protease (ThomasA) 323-878

IgA protease
MWexperimental 69 kDa
MWexpected 64 kDa
VPorod 72 nm3
log I(s) 3.14×10-2 3.14×10-3 3.14×10-4 3.14×10-5
IgA protease small angle scattering data  s, nm-1
ln I(s)
IgA protease Guinier plot ln 3.15×10-2 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
IgA protease Kratky plot 1.104 0 √3 sRg
p(r)
IgA protease pair distance distribution function Rg: 3.0 nm 0 Dmax: 9.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of IgA protease (ThomasA) 323-878 in 50 mM Tris-HCl pH 7.5, 100 mM NaCl, 2% v/v glycerol, pH 7.5 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.09464 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 55.00 μl sample at 3.0 mg/ml was injected at a 0.07 ml/min flow rate onto a GE Superdex 200 Increase 3.2/300 column at 15°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Number of frames = UNKNOWN

IgA protease
Mol. type   Protein
Organism   Thomasclavelia ramosa
Olig. state   Monomer
Mon. MW   63.7 kDa
 
UniProt   Q9AES2 (323-878)
Sequence   FASTA