Home | Research & Innovation | Scientific Programmes | Structural Biology Programme | Electron Microscopy Unit
The principal mission of the Electron Microscopy (EM) Unit is to provide scientific and technical support mainly to CNIO researchers, helping them address their scientific questions through various transmission electron microscopy techniques. We focus on sample preparation for cryo-electron microscopy (cryoEM) and negative staining methods. Our activity also includes data collection and assistance with image processing, such as 2D analysis and 3D reconstruction. We guide researchers in selecting the most appropriate EM techniques and assist with sample preparation. Additionally, we produce our own EM grids to ensure better quality control and reduce costs. Comprehensive training on the operation of our microscopes and auxiliary equipment is also available. More advanced structural studies are typically conducted through research collaborations.
The Unit has the following equipment:
- Transmition electron microscopes: 120kV Tecnai G2 Spirit (Thermo Fisher) equipped with 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 transmition electron microscope, JEM-2200FS (JEOL) with K3 direct electron detector (Gatan), ELSA holder for single sample and 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 storage cryo-grids in liquid nitrogen.
External users should contact the Head of the Unit via e-mail 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.