| MWexperimental | 30 | kDa |
| MWexpected | 34 | kDa |
| VPorod | 35 | nm3 |
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log I(s)
6.75×10-2
6.75×10-3
6.75×10-4
6.75×10-5
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s, nm-1
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Conformational multiplicity of bacterial ferric binding protein revealed by small angle x-ray scattering and molecular dynamics calculations
Liu G, Ekmen E, Jalalypour F, Mertens H, Jeffries C, Svergun D, Atilgan A, Atilgan C, Sayers Z, The Journal of Chemical Physics 158(8) (2023) DOISASDWN7 – Wild type ferric binding protein (FbpA) in apo (no Fe) form in low ionic strength (LIS) buffer (1/10 PBS)
Iron-utilization periplasmic protein|
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Fits and models
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Synchrotron SAXS
data from solutions of
Wild type ferric binding protein (FbpA) in apo (no Fe) form in low ionic strength (LIS) buffer (1/10 PBS)
in
1 mM Na2HPO4.7H2O, 0.18 mM KH2PO4, 13.7 mM NaCl, 0.27 mM KCl, 5%v/v Glycerol, pH 7.4
were collected
on the
EMBL P12 beam line
at the PETRA III storage ring
(DESY; Hamburg, Germany)
using a Pilatus 6M detector
at a sample-detector distance of 3 m and
at a wavelength of λ = 0.124 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 3.00 mg/ml was measured
at 4°C.
40 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.
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