| MWI(0) | 64 | kDa |
| MWexpected | 54 | kDa |
| VPorod | 117 | nm3 |
|
log I(s)
6.43×101
6.43×100
6.43×10-1
6.43×10-2
|
s, nm-1
|
Structural basis of myelin-associated glycoprotein adhesion and signalling.
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ, Nat Commun 7:13584 (2016) Europe PMCSASDB26 – Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) I473E mutant
Myelin-associated glycoprotein (20-508; I473E mutant)|
|
|
Fits and models
|
|
|
Synchrotron SAXS data from solutions of glycosylated myelin-associated glycoprotein (full extracellular domain (Ig1-5) I473E mutant) in HEPES, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 20°C. Nine successive 2 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 and the different curves were scaled for protein concentration.
Myelin-associated glycoprotein (MAG) full extracellular domain (immunoglobulin domains 1-5) with an I473E mutation should, based on the crystal structure, convert MAG dimers into monomers. |
|
|||||||||||||||||||||||||||||||||