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Synchrotron SAXS
data from solutions of
Native liposomes composed of lipids extracted from A/Puerto Rico/8/34 (H1N1) virus envelope loaded with M1 protein.
in
100 mM NaCl, 50 mM MES buffer, pH 6.8
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 2.00 mg/ml was measured
at 10°C.
20 successive
0.050 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 M1 matrix protein was isolated from purified influenza A/Puerto Rico/8/34(H1N1) virion.The image displays the restored electron density profile of the lipid bilayer. The additional zip file in the full entry archive contains the SAXS multiple data set of native liposomes composed of lipids extracted from A/Puerto Rico/8/34 (H1N1) virus envelope loaded with M1 protein.
Experimental small-angle scattering data are the files with extensions (*.dat).
The best fits of the SAXS curves obtained by BILMIX program are the files with extenstions (*.fit).
The restored electron density profiles of the lipid bilayer before and after loading with M1.
The molar lipid/M1 ratios are the following: (1) no M1, (2) 20:1, (3) 4:1 (4) 2.6:1.
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s, nm-1
![Native liposomes composed of lipids extracted from A/Puerto Rico/8/34 (H1N1) virus envelope loaded with M1 protein. (lipid:M1 molar ration 4:1) OTHER [STATIC IMAGE] model](/media//pdb_file/SASDMK5_electron_density.png "Static model image")
