| MWexperimental | 144 | kDa |
| MWexpected | 161 | kDa |
| VPorod | 216 | nm3 |
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log I(s)
1.79×10-1
1.79×10-2
1.79×10-3
1.79×10-4
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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) DOISASDK22 – Mammalian cell entry protein 1A (Mce1A126-454)
Mce-family protein Mce1An-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 1A (Mce1A126-454)
in
50 mM Tris, 350 mM NaCl, 10% Glycerol, 5mM DDM, 1 mM β-ME, pH 7.5
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 5.2 mg/ml was injected at a 0.15 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 Helical+Tail domain of Mammalian cell entry protein (Mce) 1A collected at DLS beamline B21 using SEC-SAXS. The molecular mass (MW) 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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