Protein crystallization promotes type 2 immunity and is reversible by antibody treatment.

Persson EK, Verstraete K, Heyndrickx I, Gevaert E, Aegerter H, Percier JM, Deswarte K, Verschueren KHG, Dansercoer A, Gras D, Chanez P, Bachert C, Gonçalves A, Van Gorp H, De Haard H, Blanchetot C, Saunders M, Hammad H, Savvides SN, Lambrecht BN, Science 364(6442) (2019) Europe PMC

SASDF86 – Human Galectin-10 (Tyr69Glu mutant)

Galectin-10 Tyr69Glu
MWexperimental 30 kDa
MWexpected 33 kDa
VPorod 46 nm3
log I(s) 1.20×10-1 1.20×10-2 1.20×10-3 1.20×10-4
Galectin-10 Tyr69Glu small angle scattering data  s, nm-1
ln I(s)
Galectin-10 Tyr69Glu Guinier plot ln 1.20×10-1 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Galectin-10 Tyr69Glu Kratky plot 1.104 0 √3 sRg
p(r)
Galectin-10 Tyr69Glu pair distance distribution function Rg: 2.2 nm 0 Dmax: 8.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Galectin-10 Tyr69Glu PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of Human Galectin-10 (Tyr69Glu mutant) in 20 mM Hepes 150 NaCl, pH 7.4 were collected on the SWING beam line at the SOLEIL storage ring (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 1.8 m and at a wavelength of λ = 0.103 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 50.00 μl sample at 20 mg/ml was injected at a 0.30 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 15°C. 14 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

Galectin-10 Tyr69Glu (Gal-10)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   16.6 kDa
 
UniProt   Q05315
Sequence   FASTA
 
PDB ID   6GKT