| MWexperimental | 142 | kDa |
| MWexpected | 146 | kDa |
| VPorod | 446 | nm3 |
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log I(s)
1.98×10-1
1.98×10-2
1.98×10-3
1.98×10-4
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s, nm-1
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Structural insights into the substrate-binding proteins Mce1A and Mce4A from Mycobacterium tuberculosis
Asthana P Singh D, Pedersen J, Hynönen M, Sulu R, Murthy A, Laitaoja M, Jänis J, Riley L, Venkatesan R, IUCrJ 8(5) (2021) DOISASDJW9 – Mammalian cell entry protein 4A (Mce4A36-400)
Mce-family protein Mce4An-Dodecyl-β-D-Maltopyranoside
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Fits and models
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Synchrotron SAXS
data from solutions of
Mammalian cell entry protein 4A (Mce4A36-400)
in
50mM Tris, 500mM NaCl, 10% Glycerol, 5mM DDM, 1mM Beta-ME, pH 8
were collected
on the
B21 beam line
at the Diamond Light Source storage ring
(Didcot, UK)
using a Pilatus 2M detector
at a wavelength of λ = 0.1 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 55.00 μl sample
at 5 mg/ml was injected at a 0.07 ml/min flow rate
onto a GE Superdex 200 Increase 3.2/300 column
.
The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Synchrotron SAXS data of the Mce+Helical+Tail domain of Mammalian cell entry protein (Mce) 4A collected at DLS beamline B21 using SEC-SAXS. The molecular mass of the protein-detergent complex was determined using Size exclusion chromatography-multi angle light scattering (SEC-MALS) coupled to refractive index measurements. The model files contain the protein-detergent molecules. The protein models were generated using iTasser and fitted against the SAXS data using the in-house program, also taking in account the micelle contribution. |
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