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Synchrotron SAXS data from solutions of deglycosylated myelin-associated glycoprotein (full extracellular domain (Ig 1-5) N406Q 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 1.90 mg/ml was measured at 4°C. 10 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 and the different curves were scaled for protein concentration.
Endo-Hf deglycosylated full extracellular domain of Myelin-associated glycoprotein (MAG) immunoglobulin domains 1-5 with an N406Q mutation that should, based on the crystal structure, enhance dimerization by removing an N-linked glycan that clashes with its symmetry mate
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s, nm-1
