| 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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