Bacterial targeting of the neutrophil inhibitory receptor LILRB3 to evade antibody immunity

SASDXG8 – Streptococcus agalactiae IgA FC receptor

IgA FC receptor β-Antigen C Protein
MWexperimental 65 kDa
MWexpected 71 kDa
VPorod 140 nm3
log I(s) 7.48×101 7.48×100 7.48×10-1 7.48×10-2
IgA FC receptor β-Antigen C Protein small angle scattering data  s, nm-1
ln I(s)
IgA FC receptor β-Antigen C Protein Guinier plot ln 7.49×101 Rg: 5.9 nm 0 (5.9 nm)-2 s2
(sRg)2I(s)/I(0)
IgA FC receptor β-Antigen C Protein Kratky plot 1.104 0 √3 sRg
p(r)
IgA FC receptor β-Antigen C Protein pair distance distribution function Rg: 5.9 nm 0 Dmax: 20.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
IgA FC receptor β-Antigen C Protein FOXSDOCK model

Synchrotron small-angle X-ray scattering (SAXS) data on Streptococcus agalactiae β-Antigen C Protein were collected at SIBYLS beamline 12.3.1 of the Advanced Light Source in SEC-SAXS mode. In-line size-exclusion chromatography (SEC) was performed using an Agilent 1260 HPLC system. The SEC conditions were as follows: a 60 µL sample at 5 mg/mL was injected onto a Shodex KW-803 column at 4 °C that had been previously equilibrated in 20 mM HEPES, 140 mM NaCl, pH 7.4, and eluted at 0.65 mL/min. Scattering was recorded on a Pilatus3 X 2M detector at a sample-to-detector distance of 2.1 m and a wavelength of λ = 0.1127 nm (I(q) vs q; q = 4π sin θ/λ, where 2θ is the scattering angle). 913 successive 2-s frames were collected. The scattering curves were normalized to the transmitted-beam intensity, radially averaged, and corrected by subtracting the solvent blank.

IgA FC receptor β-Antigen C Protein (β-Antigen C Protein)
Mol. type   Protein
Organism   Streptococcus agalactiae
Olig. state   Monomer
Mon. MW   70.9 kDa
 
UniProt   P27951 (258-826)
Sequence   FASTA