Extended disorder at the cell surface: the conformational landscape of the ectodomains of syndecans

Gondelaud F, Bouakil M, Le Fèvre A, Erica Miele A, Chirot F, Duclos B, Liwo A, Ricard-Blum S, Matrix Biology Plus :100081 (2021) DOI

SASDL69 – Ectodomain of human syndecan-1

MWexperimental 27 kDa
MWexpected 27 kDa
log I(s) 4.32×10-2 4.32×10-3 4.32×10-4 4.32×10-5
Syndecan-1 small angle scattering data  s, nm-1
ln I(s)
Syndecan-1 Guinier plot ln 4.32×10-2 Rg: 5.3 nm 0 (5.3 nm)-2 s2
Syndecan-1 Kratky plot 1.104 0 3 sRg

Data validation

Fits and models

log I(s)
 s, nm-1
Ectodomain of human syndecan-1 Rg histogram Rg, nm
Syndecan-1 EOM/RANCH model
Syndecan-1 EOM/RANCH model
Syndecan-1 EOM/RANCH model
Syndecan-1 EOM/RANCH model
Syndecan-1 EOM/RANCH model
Syndecan-1 EOM/RANCH model

Synchrotron SAXS data from solutions of Ectodomain of human syndecan-1 in 10 mM HEPES, 150 mM 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 2 m and at a wavelength of λ = 0.1033 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 7.7 mg/ml was injected at a 0.20 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 540 successive 0.990 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.

50 ul of the ectodomain of human syndecan-1 (7.7 mg/ml) were injected on a Superdex S200 Increase 5/150 GL (GE Healthcare) at a flow rate of 0.2 ml/min at 20°C. Experimental molecular weight has been determined by ESI-MS (and in solution by SEC-MALLS, estimated at 27.48 kDa).

Syndecan-1 (SDC1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   27.0 kDa
UniProt   P18827 (23-254)
Sequence   FASTA