| MWexperimental | 48 | kDa |
| MWexpected | 34 | kDa |
| VPorod | 71 | nm3 |
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log I(s)
3.19×103
3.19×102
3.19×101
3.19×100
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s, nm-1
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Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations
Nguyen G, Sutinen A, Raasakka A, Muruganandam G, Loris R, Kursula P, Frontiers in Molecular Biosciences 7 (2021) DOISASDJT8 – Monomeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358
Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆295-358|
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Fits and models
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Synchrotron SAXS data from solutions of monomeric human GDAP1∆295-358 in 25 mM HEPES, 300 mM NaCl, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 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 9 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 15°C. 3000 successive 0.045 second frames were collected through the SEC elution profile. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted from the sample elution peak frames to generate the final SAXS profile.
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