Harvard Cryo-EM Center for Structural Biology
The Harvard Cryo-Electron Microscopy Center for Structural Biology
The Harvard Cryo-Electron Microscopy Center for Structural Biology is a joint effort by Harvard Medical School, Dana-Farber Cancer Institute, Boston Children’s Hospital, Massachusetts General Hospital, and Harvard University to provide state-of-the-art cryo-EM instrumentation and expertise for the structural biology community. This user facility offers consultation and training by staff in specimen preparation, microscope operation, image acquisition, and data analysis.
Additionally, the Molecular Electron Microscopy Suite (MEMS) at Harvard Medical School is a separate user resource currently available to qualified researchers. This user facility offers training and supervision in negative-stain and cryo-transmission electron microscopy. Equipment includes three transmission electron microscopes, two cryo plungers, and sample preparation areas.
These Resources are also available to External Academic and Industrial Users!
Academic and Industry Users Welcome!
HMS Cryo-EM Facility
We welcome new academic and industry users for microscope use and training at the Cryo-EM center. See Access and Training to get started: cryoem.hms.harvard.edu/access
Start a new project at the MEMS
MEMS Facility
Many Cryo-EM projects start out with negative stain EM. Learn how to get started here: cryoem.hms.harvard.edu/mems-training
Who We Are at the HC2EM!
Recent Publications
2026
Michelle Y. Fry, Bridget E. Luce, Jonathan A. Stefely, Michael Z. Chen, Felicia G. Deng, Tiana M. Issa, Ruslan Aphasizhev, Inna Aphasizheva, Cora N. Betsinger, Steven A. Carr, Manoj T. Duraisingh, Manish Goyal, Minsoo Kim, Cameron Genxuan Lian, Yi-Ting Liao, Syed Yusuf Mian, Khanh Nguyen, Aditya S. Paul, Keith D. Rivera, Md Solayman, Namrata D. Udeshi, Andres F. Vacas, Sarah E. Calvo, John Samuelson, Vamsi K. Mootha, and Luke H. Chao. 2026. “Acanthamoeba ATP Synthase Structure Reveals the TCA Cycle Is Tethered to OXPHOS”. Cell, 189, 20, Pp. 6307-6324.e7,. doi:10.1016/j.cell.2026.08.057
Michelle Y. Fry, Bridget E. Luce, Jonathan A. Stefely, Michael Z. Chen, Felicia G. Deng, Tiana M. Issa, Ruslan Aphasizhev, Inna Aphasizheva, Cora N. Betsinger, Steven A. Carr, Manoj T. Duraisingh, Manish Goyal, Minsoo Kim, Cameron Genxuan Lian, Yi-Ting Liao, Syed Yusuf Mian, Khanh Nguyen, Aditya S. Paul, Keith D. Rivera, Md Solayman, Namrata D. Udeshi, Andres F. Vacas, Sarah E. Calvo, John Samuelson, Vamsi K. Mootha, and Luke H. Chao. 2026. “Acanthamoeba ATP Synthase Structure Reveals the TCA Cycle Is Tethered to OXPHOS”. Cell, 189, 20, Pp. 6307-6324.e7,. doi:10.1016/j.cell.2026.08.057
Rebecca J. Taylor, Karanbir S. Pahil, Alessio Caruso, Bailey Plaman, Stephen A. Early, Sebastian J. Rowe, Vadim Baidin, Andrew Wilson, Natividad Ruiz, Richard M. Walsh, Stephen C. Harrison, and Daniel Kahne. 2026. “Structural Basis for Regulating Lipopolysaccharide Transmembrane Transport”. doi:10.1038/s41586-026-11129-8
Rebecca J. Taylor, Karanbir S. Pahil, Alessio Caruso, Bailey Plaman, Stephen A. Early, Sebastian J. Rowe, Vadim Baidin, Andrew Wilson, Natividad Ruiz, Richard M. Walsh, Stephen C. Harrison, and Daniel Kahne. 2026. “Structural Basis for Regulating Lipopolysaccharide Transmembrane Transport”. doi:10.1038/s41586-026-11129-8
Sayan Chakraborty, Jie Jiang, Javier Vinals Camallonga, Dimitris Gazgalis, Thomas W. Gero, Maurício T. Tavares, Georgia Dittemore, Emre Tkacik, Tyler S. Beyett, Dong Man Jang, Byung Hak Ha, Felix H. Gottlieb, Talya Levitz, Rebecca J. Metivier, Anna M. Schmoker, David A. Scott, Hyesung Jeon, Pasi A. Jänne, and Michael J. Eck. 2026. “RAF Isoform Selectivity of MEK Inhibitors and Rational Design of a Covalent ARAF-MEK Inhibitor”. Science Advances, 12, Pp. eaee5241. doi:10.1126/sciadv.aee5241
Sayan Chakraborty, Jie Jiang, Javier Vinals Camallonga, Dimitris Gazgalis, Thomas W. Gero, Maurício T. Tavares, Georgia Dittemore, Emre Tkacik, Tyler S. Beyett, Dong Man Jang, Byung Hak Ha, Felix H. Gottlieb, Talya Levitz, Rebecca J. Metivier, Anna M. Schmoker, David A. Scott, Hyesung Jeon, Pasi A. Jänne, and Michael J. Eck. 2026. “RAF Isoform Selectivity of MEK Inhibitors and Rational Design of a Covalent ARAF-MEK Inhibitor”. Science Advances, 12, Pp. eaee5241. doi:10.1126/sciadv.aee5241
Zishuo Yu, Pradeep Sathyanarayana, Joel M. J. Tan, Side Hu, Xiaoyi Fan, Angela Gao, Philip J. Kranzusch, Joseph J. Loparo, and Jonathan Abraham. 2026. “Structure and Operating Principles of a Monkeypox Virus Replisome”. doi:10.1038/s41586-026-10937-2
Zishuo Yu, Pradeep Sathyanarayana, Joel M. J. Tan, Side Hu, Xiaoyi Fan, Angela Gao, Philip J. Kranzusch, Joseph J. Loparo, and Jonathan Abraham. 2026. “Structure and Operating Principles of a Monkeypox Virus Replisome”. doi:10.1038/s41586-026-10937-2
Marilina de Sautu, Conny Leistner, Tomas Kirchhausen, Simon Jenni, and Stephen C. Harrison. 2026. “Mechanism of Membrane Perforation in Rotavirus Cell Entry”. Science, 393, Pp. 1128-33. doi:10.1126/science.aeg4851
Marilina de Sautu, Conny Leistner, Tomas Kirchhausen, Simon Jenni, and Stephen C. Harrison. 2026. “Mechanism of Membrane Perforation in Rotavirus Cell Entry”. Science, 393, Pp. 1128-33. doi:10.1126/science.aeg4851
Haixia Zhou, Lea Terbeck, Andrew Berical, Marine Brunet, Sven M. Lange, Jacob R. Anderson, Heike Olbrich, Diana Carolin Bracht, Kai Wohlgemuth, Cynthia Rieck, Johanna Raidt, Jürgen Klingauf, Sivagurunathan Sutharsan, Huda Mussaffi, Dario Prais, Victoria Dunphy, Sachiko T. Homma, Paul Guichard, Virginie Hamel, Finn J. Hawkins, Heymut Omran, and Alan Brown. 2026. “In Situ Structure of the Human Ciliary Transition Zone Links Linker Defects to Primary Ciliary Dyskinesia”. Science, Pp. eaei5957. doi:10.1126/science.aei5957
Haixia Zhou, Lea Terbeck, Andrew Berical, Marine Brunet, Sven M. Lange, Jacob R. Anderson, Heike Olbrich, Diana Carolin Bracht, Kai Wohlgemuth, Cynthia Rieck, Johanna Raidt, Jürgen Klingauf, Sivagurunathan Sutharsan, Huda Mussaffi, Dario Prais, Victoria Dunphy, Sachiko T. Homma, Paul Guichard, Virginie Hamel, Finn J. Hawkins, Heymut Omran, and Alan Brown. 2026. “In Situ Structure of the Human Ciliary Transition Zone Links Linker Defects to Primary Ciliary Dyskinesia”. Science, Pp. eaei5957. doi:10.1126/science.aei5957
Paula P. Navarro, Andrea Vettiger, Roman Hajdu, Virly Y. Ananda, Alejandro López-Tavares, Ernst W. Schmid, Johannes C. Walter, Martin Loose, Luke H. Chao, and Thomas G. Bernhardt. 2026. “The Penicillin-Binding Protein PBP1b Fortifies the Escherichia Coli Division Site Against Osmotic Rupture”, 11, 8, Pp. 2142-2156,. doi:10.1038/s41564-026-02403-6
Paula P. Navarro, Andrea Vettiger, Roman Hajdu, Virly Y. Ananda, Alejandro López-Tavares, Ernst W. Schmid, Johannes C. Walter, Martin Loose, Luke H. Chao, and Thomas G. Bernhardt. 2026. “The Penicillin-Binding Protein PBP1b Fortifies the Escherichia Coli Division Site Against Osmotic Rupture”, 11, 8, Pp. 2142-2156,. doi:10.1038/s41564-026-02403-6
Hojong Yoon, Franziska Wachter, Katharine A. Barrett, Cyrus Jin, Anna Rodríguez-Pöhnlein, Justine C. Rutter, Ryan J. Lumpkin, Rebecca J. Metivier, Katherine A. Donovan, Kheewoong Baek, Yongying Jiang, Minwoo Lee, Robert W. Kalis, Jianwei Che, Yuan Xiong, Eric S. Fischer, and Benjamin L. Ebert. 2026. “DCAF11-Dependent Molecular Glue Degrader Activated by Glutathionylation”. doi:10.1038/s41586-026-10873-1
Hojong Yoon, Franziska Wachter, Katharine A. Barrett, Cyrus Jin, Anna Rodríguez-Pöhnlein, Justine C. Rutter, Ryan J. Lumpkin, Rebecca J. Metivier, Katherine A. Donovan, Kheewoong Baek, Yongying Jiang, Minwoo Lee, Robert W. Kalis, Jianwei Che, Yuan Xiong, Eric S. Fischer, and Benjamin L. Ebert. 2026. “DCAF11-Dependent Molecular Glue Degrader Activated by Glutathionylation”. doi:10.1038/s41586-026-10873-1