| MWexperimental | 16 | kDa |
| MWexpected | 17 | kDa |
| VPorod | 29 | nm3 |
|
log I(s)
2.34×10-2
2.34×10-3
2.34×10-4
2.34×10-5
|
s, nm-1
|
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) DOISASDJU9 – Mammalian cell entry protein 1A (Mce1A36-148)
Mce-family protein Mce1A monomer|
|
|
Fits and models
|
|
|
|
|
|
|
Synchrotron SAXS
data from solutions of
Mammalian cell entry protein 1A (Mce1A36-148)
in
50 mM Tris, 350 mM NaCl, 10% Glycerol, pH 8.5
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).
One solute concentration of 2.00 mg/ml was measured
at 4°C.
28 successive
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.
Synchrotron SAXS data of the Mce domain of Mammalian cell entry protein (Mce) 1A collected at DLS beamline B21 using batch mode method. The molecular mass was determined using Size exclusion chromatography-multi angle light scattering (SEC-MALS) coupled to refractive index measurements and also with the SAXS data. The protein models were generated using Robetta- template based modeling by using Mce4A39-140 crystal structure as the template and fitted against the SAXS data using the in-house program. |
|
|||||||||||||||||||||||||||