TEM Glacios 200kV: Falcon 4i Camera + Selectris X Energy Filter

Thermofisher Glacios at the AFMB lab
Apoferritin structure at 1.9Å-resolution solved during CWAT
Alpha helix element of apoferritin

Cryo-EM field has been developing with unprecedented pace. Modern TEM allows collect data with increasing speed and high efficient robotic systems integrated in the microscope enable multiple experiments that can be done in fully automated non-assisted fashion. The EM workflow on modern microscopes is perfectly reliable and optimally set for quick evaluation of sample quality and setting up data acquisition.

AFMB has recently upgraded its cryo-EM facility with new Glacios 200kV TEM allowing efficient screening of samples and high resolution data collection. The AFMB Glacios has the most modern configuration and the best performance achievable on a 200kV TEM. New generation camera Falcon4i and an energy filter Selectris X available on our microscope account for unbeatable acquisition speed and image quality.

Performance tests conducted at Thermofisher factory during CWAT demonstrate that a resolution better than 1.9A can be achieved on our instrument (apoferritin). The instrument is also suitable for tilt series collection for cryo-electron tomography on thin samples (thickness <150nm) such as lamella or particles in solution (including vesicles).

We welcome users from any life sciences labs. Assistance is offered during sample preparation and imaging sessions. Users can benefit from a prep lab at AFMB if any additional preparations need to be done to the samples. For grid freezing there are Vitrobot Mark4 and Leica GP available to users.

Advanced EM users can also benefit from training offered by the platform. The training program can be tailored to specific user demands.

While high-end microscope is available at our facility we strongly recommend users to test their samples by negative staining EM on a Tecnai 120 that is also available at our lab.

No prior assessment of projects is necessary to access our facility but we do advise to get in touch with the facility manager to discuss the project before planning cryo-EM work.

How to access?

Publications associated with this facility

    • Nilsson J, Baroudi H, Gondelaud F, Pesce G, Bignon C, Ptchelkine D, Chamiech J, Cottet Hervé, Kajava A, Longhi S (2023) Molecular Determinants of Fibrillation in a Viral Amyloidogenic Domain from Combined Biochemical and Biophysical Studies. Int J Mol Sci 24:399*

    • Pesce G, Gondelaud F, Ptchelkine D, Nilsson J, Bignon C, Cartalas J, Fourquet P, Longhi S (2022) Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins Int J Mol Sci 23:923

    • Gondelaud F, Pesce G, Nilsson J, Bignon C, Ptchelkine D, Gerlier D, Mathieu C, Longhi S (2022) Functional benefit of structural disorder for the replication of measles, Nipah and Hendra viruses. Essays in Bioc 66:915-934

    • 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.