| MWI(0) | 67 | kDa |
| MWexpected | 121 | kDa |
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log I(s)
4.80×10-2
4.80×10-3
4.80×10-4
4.80×10-5
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s, nm-1
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Small-angle neutron scattering studies suggest the mechanism of BinAB protein internalization
Sharma M, Aswal V, Kumar V, Chidambaram R, IUCrJ 7(2) (2020) DOISASDF97 – Complex of Binary toxin receptor (Cqm1) with deuterated BinB component protein in 100% D2O
Binary toxin receptor Cqm1 proteinDeuterated BinB component of mosquito-larvicidal Binary toxin
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Fits and models
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SANS
data from solutions of
Complex of Binary toxin receptor (Cqm1) with deuterated BinB component protein in 100% D2O
in
25 mM HEPES, pH 7.5, 25 mM NaCl, in 100% D2O, pH 7.5
were collected
using a 1 m long He3 position sensitive detector detector
at a sample-detector distance of 2 m and
at a wavelength of λ = 0.52 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 1.00 mg/ml was measured
at 25°C.
One
43200 second frame was collected.
The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
This data is for a stable complex of receptor Cqm1 protein and deuterated BinB component of mosquito-larvicidal Binary (BinAB) toxin. Deuterated BinB (dBinB) protein was synthesized using E. coli based protein expression system grown in M9+ medium in D2O after three step adaption. The extent of deuteration for dBinB was estimated from contrast (p − s)2 values to be ~77%. Theoretical molecular weight of the dBinB protein includes 77% of D atoms. SANS analysis (DAMMIN and CRYSON fit) suggest that deuterated BinB (dBinB), expectedly, is fully matched out against the used solvent (100% D2O) and only monomer of Cqm1 is modelled from SANS experiments |
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