| MWexperimental | 47 | kDa |
| MWexpected | 49 | kDa |
| VPorod | 70 | nm3 |
|
log I(s)
4.88×103
4.88×102
4.88×101
4.88×100
|
s, nm-1
|
Structural plasticity of NFU1 upon interaction with binding partners: insights into the mitochondrial [4Fe-4S] cluster pathway
Da Vela S, Saudino G, Lucarelli F, Banci L, Svergun D, Ciofi-Baffoni S, Journal of Molecular Biology :168154 (2023) DOISASDPD8 – Human apo iron-sulfur cluster assembly 1/iron-sulfur cluster assembly 2/NFU1 iron-sulfur cluster scaffold protein complex (ISCA1-ISCA2-NFU1)
Iron-sulfur cluster assembly 1 homolog, mitochondrialNFU1 iron-sulfur cluster scaffold homolog, mitochondrial (F118S, E168G)
Iron-sulfur cluster assembly 2 homolog, mitochondrial
|
|
|
Fits and models
|
|
|
|
|
Synchrotron SAXS data from solutions of the ISCA1-ISCA2-NFU1 complex in 50 mM phosphate, 150 mM NaCl, 5 mM DTT, pH 7 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 3.1 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 30.00 μl sample at 20.4 mg/ml was injected at a 0.30 ml/min flow rate onto a GE Superdex 75 Increase 5/150 column at 20°C. 900 successive 0.995 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.
|
|
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||