Transmission electron microscopy
This PBSIM service permits the structural characterization of biological systems and large macromolecular assemblies, as a complementary approach to x-ray crystallography.
The service allows users to perform all steps for the preparation of biological samples by negative staining to enable high contrast imaging form naturally low-contrast objects, imaging acquisition on the embedded camera and image analysis. This approach can be used to characterize the structural homogeneity of a protein sample, generate a low resolution 3D structure or identify large conformational changes in proteins or complexes upon addition of ligands.
You can find this service in these videos: https://www.youtube.com/watch?v=E-5vKfjZoPA&list=PLhk31IqVPY96UXlRAOGLuz_PyGCFnpGDp&index= and https://www.youtube.com/watch?v=Q60zzro4tDw&list=PLhk31IqVPY96UXlRAOGLuz_PyGCFnpGDp&index=7
Accessibility
Academia and industries
Cost
To be defined from the service requested
How to access?
- Complete the proposal from
and check “Marseille” for the “Electron microscopy” item - Contact AFMB: Denis Ptchelkine
Specific equipment
- 1 FEI Tecnai G2 spirit 120 kV equipped with a low dose module and a 2k x 2k CCD camera
Team contacts
Publications associated with this facility
- Bebeacua C, Tremblay D, Farenc C, Chapot-Chartier MP, Sadovskaya I, van Heel M, Veesler D, Moineau S, Cambillau C (2013) Structure, adsorption to host, and infection mechanism of virulent lactococcal phage p2. J Virol 87:12302-12.
- Desmyter A, Farenc C, Mahony J, Spinelli S, Bebeacua C, Blangy S, Veesler D, van Sinderen D, Cambillau C (2013) Viral infection modulation and neutralization by camelid nanobodies. Proc Natl Acad Sci U S A 110:E1371-9.
- Sciara G, Bebeacua C, Bron P, Tremblay D, Ortiz-Lombardia M, Lichière J, van Heel M, Campanacci V, Moineau S, Cambillau C (2010) Structure of lactococcal phage p2 baseplate and its mechanism of activation. Proc Natl Acad Sci USA 10:6852-7.
- Bignon C, Li C, Lichière J, Canard B, Coutard B (2013) Improving the soluble expression of recombinant proteins by randomly shuffling 5’ and 3’ coding-sequence ends. Acta Crystallogr D 69, 2580-2.
- Le Breton M, Meyniel-Schicklin L, Deloire A, Coutard B, Canard B, de Lamballerie X, Andre P, Rabourdin-Combe C, Lotteau V, Davoust N (2011) Flavivirus NS3 and NS5 proteins interaction network : a high-throughput yeast two-hybrid screen. BMC Microbiol 11, 234.
