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

SASDC76 – Extracellular domain of human B-lymphocyte cell receptor CD22

CD22 extracellular domain
MWexperimental 90 kDa
MWexpected 90 kDa
log I(s) 3.46×10-1 3.46×10-2 3.46×10-3 3.46×10-4
CD22 extracellular domain small angle scattering data  s, nm-1
ln I(s)
CD22 extracellular domain Guinier plot ln 3.46×10-1 Rg: 8.0 nm 0 (8.0 nm)-2 s2
(sRg)2I(s)/I(0)
CD22 extracellular domain Kratky plot 1.104 0 3 sRg
p(r)
CD22 extracellular domain pair distance distribution function Rg: 8.4 nm 0 Dmax: 30.6 nm

Data validation


Fits and models


log I(s)
 s, nm-1
CD22 extracellular domain DAMMIF model

Synchrotron SAXS data from solutions of Extracellular domain of human B-lymphocyte cell receptor CD22 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 = 0.0886 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