| MWexperimental | 43 | kDa |
| MWexpected | 56 | kDa |
| VPorod | 55 | nm3 |
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log I(s)
4.55×101
4.55×100
4.55×10-1
4.55×10-2
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s, nm-1
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The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc.
Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D, Falconi M, Chiancone E, Biochim Biophys Acta 1840(1):535-44 (2014) Europe PMCSASDA35 – SeZinT-SeZnuA complex
High-affinity zinc transporter periplasmic componentZinc/cadmium-binding protein
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Fits and models
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Synchrotron SAXS
data from solutions of
SeZinT-SeZnuA complex
in
50 mM HEPES 50 mM KCl, pH 7.5
were collected
on the
BM29 beam line
at the ESRF storage ring
(Grenoble, France)
using a Pilatus 1M detector
at a sample-detector distance of 2.4 m and
at a wavelength of λ = 0.93 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
Solute concentrations ranging between 0.2 and 5 mg/ml were measured
at 4°C.
10 successive
1 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.
The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
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