Molecular basis of human CD22 function and therapeutic targeting.

Ereño-Orbea J, Sicard T, Cui H, Mazhab-Jafari MT, Benlekbir S, Guarné A, Rubinstein JL, Julien JP, Nat Commun 8(1):764 (2017) Europe PMC

SASDC86 – Extracellular domain of human B-lymphocyte cell receptor CD22 in complex with alpha 2,6 sialyllactose

CD22 extracellular domain
alpha(2,6)-Sialyllactose
MWexperimental 90 kDa
MWexpected 91 kDa
log I(s) 3.06×10-1 3.06×10-2 3.06×10-3 3.06×10-4
CD22 extracellular domain alpha(2,6)-Sialyllactose small angle scattering data  s, nm-1
ln I(s)
CD22 extracellular domain alpha(2,6)-Sialyllactose Guinier plot ln 3.07×10-1 Rg: 8.1 nm 0 (8.1 nm)-2 s2
(sRg)2I(s)/I(0)
CD22 extracellular domain alpha(2,6)-Sialyllactose Kratky plot 1.104 0 √3 sRg
p(r)
CD22 extracellular domain alpha(2,6)-Sialyllactose pair distance distribution function Rg: 8.5 nm 0 Dmax: 29.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
CD22 extracellular domain alpha(2,6)-Sialyllactose DAMMIF model
Synchrotron SAXS data from solutions of Extracellular domain of human B-lymphocyte cell receptor CD22 in complex with alpha 2,6 sialyllactose in 20 mM Tris 150 mM NaCl, pH 9 were collected on the 12-ID-B SAXS/WAXS beam line at the Advanced Photon Source (APS), Argonne National Laboratory storage ring (Lemont, IL, USA) using a Pilatus 2M detector at a sample-detector distance of 3.6 m and at a wavelength of λ = 0.08856 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 22°C. 30 successive 1 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.

Storage temperature = UNKNOWN

CD22 extracellular domain (CD22)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   90 kDa
 
UniProt   P20273
Sequence   FASTA
 
alpha(2,6)-Sialyllactose
Mol. type   Other
Olig. state   Unknown
Mon. MW   0.6 kDa