| MWexperimental | 121 | kDa |
| MWexpected | 90 | kDa |
| VPorod | 204 | nm3 |
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log I(s)
2.12×102
2.12×101
2.12×100
2.12×10-1
|
s, nm-1
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Structural and biophysical insights into RomR, MglB and MglC interactions involved in regulating cell polarity in Myxococcus xanthus
Kodesia A, Kapoor S, Thakur K, Journal of Biological Chemistry :110907 (2025) DOISASDXU4 – Mutual gliding motility protein C and B interacting with the C-terminal helix of RomR protein from Myxococcus xanthus
Two-component system response regulatorMutual gliding motility protein C
Gliding motility protein MglB
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Fits and models
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Synchrotron SAXS
data from solutions of
Mutual gliding motility protein C and B interacting with the C-terminal helix of RomR protein from Myxococcus xanthus
in
20 mM HEPES, 150 mM NaCl, 10% glycerol, pH 8
were collected
on the
BM29 beam line
at the ESRF storage ring
(Grenoble, France)
using a Pilatus3 2M detector
at a sample-detector distance of 2.8 m and
at a wavelength of λ = 0.0991 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 50.00 μl sample
at 1 mg/ml was injected at a 0.60 ml/min flow rate
onto a Agilent AdvanceBio SEC 300Å, 4.6 x 150 mm column
at 4°C.
750 successive
2 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.
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