| MWexperimental | 33 | kDa |
| MWexpected | 59 | kDa |
| VPorod | 33 | nm3 |
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log I(s)
1.24×10-1
1.24×10-2
1.24×10-3
1.24×10-4
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s, nm-1
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Insight into the structure and interactions of the M. tuberculosis Mce-associated membrane proteins Mam1A-1D
Hynönen M, Perumal P, Hynönen N, Doutch J, Ma K, Venkatesan R, (2025) DOISASDXG2 – Probable conserved Mce associated membrane protein (Mam1Adelta106) from M.tuberculosis (SANS)
Probable conserved Mce associated membrane protein|
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Fits and models
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SANS
data from solutions of
Probable conserved Mce associated membrane protein (Mam1Adelta106) from M.tuberculosis (SANS)
in
50 mM Tris, 500 mM NaCl, D-C12E9, pH 8.5
were collected
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
at 6°C.
The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
SANS data were collected on the Zoom time-of-flight SANS instrument (ISIS Neutron and Muon Source, Harwell, UK) using wavelength range 1.75-16.5Å. The source to sample and sample to detector distance was 4 m and the beam size was 12 mm. Mam1Adelta106 was solubilized with C12E9 in the lysis buffer where the deuteration of the C12E9 was 0.2 % v/v. Excess C12E9 was washed away throughout the purification, and replaced with D-C12E9 in the STFC SANS facilities using SEC Superdex200 column. From the highest point of the peak, 3 fractions were selected. Each of these fractions was loaded to Starna Scientific quartz round cuvette (match code 6,path length 1, type 32/Q/1), and SANS data were collected from each fraction with an exposure time of 1 h in 5 cycles (5 h total exposure time for each fraction). The neutron momentum transfer (q) standard deviation is provided as an additional file. |
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