Structural insights into the contactin 1 – neurofascin 155 adhesion complex

Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B, Nature Communications 13(1) (2022) DOI

SASDLC6 – High mannose neurofascin 155 immunoglobulin domains 1-6, 1.3 μM

Neurofascin
MWI(0) 81 kDa
MWexpected 139 kDa
VPorod 172 nm3
log I(s) 5.73×10-3 5.73×10-4 5.73×10-5 5.73×10-6
Neurofascin small angle scattering data  s, nm-1
ln I(s)
Neurofascin Guinier plot ln 5.74×10-3 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
Neurofascin Kratky plot 1.104 0 √3 sRg
p(r)
Neurofascin pair distance distribution function Rg: 3.9 nm 0 Dmax: 12.6 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of High mannose neurofascin 155 immunoglobulin domains 1-6, 1.3 μM in 25 mM HEPES, 150 mM NaCl, pH 7.5 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.09 mg/ml was measured. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

High mannose neurofascin 155 immunoglobulin domains 1-6 1.3 μM. Experimental molecular weight=Sequence Expected MW + MW for 4 N glycosylation sites confirmed crystallographically. X-ray wavelength: UNKNOWN. X-ray exposure time: UNKNOWN. Experimental temperature: UNKNOWN.

Neurofascin
Mol. type   Protein
Organism   Mus musculus
Olig. state   Dimer
Mon. MW   69.5 kDa
 
UniProt   E9PW06 (25-621)
Sequence   FASTA