Home | Research & Innovation | Scientific Programmes | Structural Biology Programme | Electron Microscopy Unit
The main goal of the Electron Microscopy (EM) Unit is to provide scientific-technical support to researchers to resolve their scientific questions using different transmission EM techniques. Sample preparation is routinely carried out using cryo-EM and negative staining methods. We also perform data collection and assist with image processing, including 2D analysis and 3D reconstruction. We offer guidance in choosing the most suitable EM techniques and assist with all aspects of sample preparation. Furthermore, we manufacture our own sample supports (EM grids), ensuring improved quality control while lowering operational costs. We also offer comprehensive training for the use of our microscopes and associated equipment. Advanced structural analyses are generally carried out through research collaborations.
The Unit has the following equipment:
- Transmission electron microscopes: 120 kV Tecnai G2 Spirit (Thermo Fisher) equipped with a CCD camera, TemCam-F416 (TVIPS) and cryo-holders for one and three samples (Gatan 626 for one sample and Gatan 910 for three samples).
- 200 kV transmission electron microscope, JEM-2200FS (JEOL), with a K3 direct electron detector (Gatan), ELSA holder for a single sample, and a 910 holder for three samples (Gatan).
- High-speed sample vitrification prototype (RAPIDO).
- Semi-automated vitrification device Vitrobot Mark IV (Thermo Fisher).
- Glow Discharge GloQube (Quorum Technologies).
- Evaporator E6700 (Polaron).
- Two Dewars with four racks (SubAngstrom) for storing cryo-grids in liquid nitrogen.
External users should contact the Head of the Unit via email jboskovic@cnio.es in order to arrange the use of the equipment.
Recent publications
- Martín-Hurtado A, Contreras J, Sánchez-Wandelmer J, Zarzuela E, García F, Le Coq J, Boskovic J, Muñoz IG, Gago F, Muñoz J, Isasa M, Plaza-Menacho I. (2026). The oncogenic CCDC6-RET fusion protein is a dual ATP- and ADP-dependent kinase. Nat Commun (in press). CNIO Publication.
- Palacios-Abella A, López-Perrote A, Boskovic J, Fonseca S, Úrbez C, Rubio V, Llorca O, Alabadí D. (2025). The structure of the R2T complex reveals a different architecture from the related HSP90 cochaperone R2TP. Structure 33, 740-752. CNIO Publication.
- García- Martín C, López-Perrote A, Boskovic J , Llorca O (2024). Mechanism of allosteric inhibition of RUVBL1-RUVBL2 ATPase by the small molecule CB-6644. Cell Rep Phys Sci 5, 101982. CNIO Publication.
- Rivera-Calzada A, Arribas-Bosacoma R, Ruiz-Ramos A, Escudero-Bravo P, Boskovic J, Fernandez-Leiro R, Oliver AW, Pearl LH, Llorca O. (2022). Structural basis for the inactivation of cytosolic DNA sensing by the vaccinia virus.. Nat Commun 13, 7062. CNIO Publication.
Open Access - Rodriguez CF, Escudero-Bravo P, Díaz L, Bartoccioni P, García-Martín C, Gilabert JG, Boskovic J, Guallar V, Errasti-Murugarren E, Llorca O, Palacín M (2021). Structural basis for substrate specificity of heteromeric transporters of neutral amino acids.. Proc Natl Acad Sci USA 118, e2113573118. CNIO Publication.
- Villasante A, Godier-Furnemont A, Hernandez-Barranco A, Coq JL, Boskovic J, Peinado H, Mora J, Samitier J, Vunjak-Novakovic G (2021). Horizontal transfer of the stemness-related markers EZH2 and GLI1 by neuroblastoma-derived extracellular vesicles in stromal cells. Transl Res 237, 82-97. CNIO Publication.
- Le Coq J, López Navajas P, Rodrigo Martin B, Alfonso C, Lietha D (2021). A new layer of phosphoinositide-mediated allosteric regulation uncovered for SHIP2.. FASEB J 35, e21815. CNIO Publication.