# 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!** ![50 structures](/sites/g/files/omnuum8871/files/styles/hwp_21_9__1920x825/public/2025-04/50ish_structures.jpg?itok=koDBjYIL) [### Academic and Industry Users Welcome! ](/access)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](https://cryoem.hms.harvard.edu/access) ![instruments3](/sites/g/files/omnuum8871/files/styles/hwp_16_9__480x270/public/cryo-em.hms.harvard.edu/files/screen_shot_2021-05-22_at_2.14.06_pm_0.png?itok=IuD6AkpT) [### Start a new project at the MEMS ](/mems-training)MEMS Facility Many Cryo-EM projects start out with negative stain EM. Learn how to get started here: [cryoem.hms.harvard.edu/mems-training](https://cryoem.hms.harvard.edu/mems-training) ![cryoem](/sites/g/files/omnuum8871/files/styles/hwp_16_9__480x270/public/cryo-em.hms.harvard.edu/files/nocyto_virus_0.png?itok=AAVIztdd) ## Who We Are at the HC2EM! ## Recent Publications Download 8 citations download- [BibTeX](/bibcite/export?pager_style=no_pager&number_of_items=8&sort_field=bibcite_year--desc&taxonomy_filters=&&&format=bibtex) - [EndNote X3 XML](/bibcite/export?pager_style=no_pager&number_of_items=8&sort_field=bibcite_year--desc&taxonomy_filters=&&&format=endnote8) - [EndNote 7 XML](/bibcite/export?pager_style=no_pager&number_of_items=8&sort_field=bibcite_year--desc&taxonomy_filters=&&&format=endnote7) - [Endnote tagged](/bibcite/export?pager_style=no_pager&number_of_items=8&sort_field=bibcite_year--desc&taxonomy_filters=&&&format=tagged) - [Marc](/bibcite/export?pager_style=no_pager&number_of_items=8&sort_field=bibcite_year--desc&taxonomy_filters=&&&format=marc) - [PubMedId](/bibcite/export?pager_style=no_pager&number_of_items=8&sort_field=bibcite_year--desc&taxonomy_filters=&&&format=pubmed_id) - [RIS](/bibcite/export?pager_style=no_pager&number_of_items=8&sort_field=bibcite_year--desc&taxonomy_filters=&&&format=ris) ### 2026 Della Syau, Felix Steinruecke, Sophie Roth, Ernst Schmid, Karen Adelman, Johannes C Walter, and Lucas Farnung. 2026. “[Structure and Function of IWS1 in Transcription Elongation](/publication/structure-and-function-iws1-transcription-elongation)”. Nucleic Acids Research, 54, Pp. gkag357. doi:10.1093/nar/gkag357 Della Syau, Felix Steinruecke, Sophie Roth, Ernst Schmid, Karen Adelman, Johannes C Walter, and Lucas Farnung. 2026. “[Structure and Function of IWS1 in Transcription Elongation](/publication/structure-and-function-iws1-transcription-elongation)”. Nucleic Acids Research, 54, Pp. gkag357. doi:10.1093/nar/gkag357 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://doi.org/10.1093/nar/gkag357) Transcription elongation by RNA polymerase II is a tightly regulated process that requires coordinated interactions between transcription elongation factors. IWS1 (Interacts with SPT6) has been implicated as a core elongation factor, but its molecular... - [ descriptionPublisher's Version](https://doi.org/10.1093/nar/gkag357) Benjamin D. Thomson, Melissa D. Marquez, Shaun Rawson, Thiago M. A. dos Santos, Stephen C. Harrison, and Daniel Kahne. 2026. “[Structures of Folding Intermediates on BAM Show Diverse Substrates Fold by a Conserved Mechanism](/publication/structures-folding-intermediates-bam-show-diverse-substrates-fold-conserved-mechanism)”. Proceedings of the National Academy of Sciences, 123, Pp. e2534936123. doi:10.1073/pnas.2534936123 Benjamin D. Thomson, Melissa D. Marquez, Shaun Rawson, Thiago M. A. dos Santos, Stephen C. Harrison, and Daniel Kahne. 2026. “[Structures of Folding Intermediates on BAM Show Diverse Substrates Fold by a Conserved Mechanism](/publication/structures-folding-intermediates-bam-show-diverse-substrates-fold-conserved-mechanism)”. Proceedings of the National Academy of Sciences, 123, Pp. e2534936123. doi:10.1073/pnas.2534936123 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://www.pnas.org/doi/abs/10.1073/pnas.2534936123) The outer membrane of Gram-negative bacteria contains a wide variety of integral β-barrel proteins. Here, we study the conserved β-barrel assembly machine which is responsible for folding and inserting these membrane β-barrels. By determining the... - [ descriptionPublisher's Version](https://www.pnas.org/doi/abs/10.1073/pnas.2534936123) Sonomi Yamaguchi, Samantha G. Fernandez, Douglas R. Wassarman, Marlen Lüders, Frank Schwede, and Philip J. Kranzusch. 2026. “[Nucleotide Signals Coordinate Activation and Inhibition of Bacterial Immunity](/publication/nucleotide-signals-coordinate-activation-and-inhibition-bacterial-immunity)”, 652, 8111, Pp. 978-985,. doi:10.1038/s41586-026-10135-0 Sonomi Yamaguchi, Samantha G. Fernandez, Douglas R. Wassarman, Marlen Lüders, Frank Schwede, and Philip J. Kranzusch. 2026. “[Nucleotide Signals Coordinate Activation and Inhibition of Bacterial Immunity](/publication/nucleotide-signals-coordinate-activation-and-inhibition-bacterial-immunity)”, 652, 8111, Pp. 978-985,. doi:10.1038/s41586-026-10135-0 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://doi.org/10.1038/s41586-026-10135-0) The cellular nucleotide pool is a major focal point of the host immune response to viral infection. Immune effector proteins that disrupt the nucleotide pool enable animal and bacterial cells to broadly restrict diverse viruses, but reduced nucleotide... - [ descriptionPublisher's Version](https://doi.org/10.1038/s41586-026-10135-0) Nathalie R. Lavoie and Ekaterina E. Heldwein. 2026. “[Reproducible Sample Preparation of Virus-Infected Cells for Cryo-FIB ET Using Manual Plunge Freezing](/publication/reproducible-sample-preparation-virus-infected-cells-cryo-fibet-using-manual-plunge)”. Bio-protocol, 16, 1, Pp. e5563+. doi:10.21769/BioProtoc.5563 Nathalie R. Lavoie and Ekaterina E. Heldwein. 2026. “[Reproducible Sample Preparation of Virus-Infected Cells for Cryo-FIB ET Using Manual Plunge Freezing](/publication/reproducible-sample-preparation-virus-infected-cells-cryo-fibet-using-manual-plunge)”. Bio-protocol, 16, 1, Pp. e5563+. doi:10.21769/BioProtoc.5563 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://doi.org/10.21769/BioProtoc.5563) Most viruses extensively remodel their host cells to establish productive infection. Visualization of virus-induced cellular remodeling by electron microscopy (EM) has been revolutionized in recent years by advances in cryo-focused ion beam (cryo-FIB)... - [ descriptionPublisher's Version](https://doi.org/10.21769/BioProtoc.5563) Zishuo Yu, Pradeep Sathyanarayana, Cong Liu, Joel M.J. Tan, Pan Yang, Biswajit Das, Side Hu, Xiaoyi Fan, Chenggong Ji, Sandra K. Weller, Mrinal Shekhar, Donald M. Coen, Philip J. Kranzusch, Joseph J. Loparo, and Jonathan Abraham. 2026. “[Mechanisms of HSV-1 Helicase-Primase Inhibition and Replication Fork Complex Assembly](/publication/mechanisms-hsv-1-helicase-primase-inhibition-and-replication-fork-complex-assembly-0)”. Cell, 189, 2, Pp. 478-494.e18,. doi:10.1016/j.cell.2025.11.041 Zishuo Yu, Pradeep Sathyanarayana, Cong Liu, Joel M.J. Tan, Pan Yang, Biswajit Das, Side Hu, Xiaoyi Fan, Chenggong Ji, Sandra K. Weller, Mrinal Shekhar, Donald M. Coen, Philip J. Kranzusch, Joseph J. Loparo, and Jonathan Abraham. 2026. “[Mechanisms of HSV-1 Helicase-Primase Inhibition and Replication Fork Complex Assembly](/publication/mechanisms-hsv-1-helicase-primase-inhibition-and-replication-fork-complex-assembly-0)”. Cell, 189, 2, Pp. 478-494.e18,. doi:10.1016/j.cell.2025.11.041 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://doi.org/10.1016/j.cell.2025.11.041) Herpesviruses are widespread double-stranded DNA viruses that establish lifelong latency and cause various diseases. Although DNA-polymerase-targeting antivirals are effective, increasing drug resistance underscores the need for alternatives. Helicase... - [ descriptionPublisher's Version](https://doi.org/10.1016/j.cell.2025.11.041) ### 2025 2025. “[Molecular Organization of the New World Arenavirus Spike Glycoprotein Complex](/publication/molecular-organization-new-world-arenavirus-spike-glycoprotein-complex-0)”. doi:10.1038/s41564-025-02085-6 2025. “[Molecular Organization of the New World Arenavirus Spike Glycoprotein Complex](/publication/molecular-organization-new-world-arenavirus-spike-glycoprotein-complex-0)”. doi:10.1038/s41564-025-02085-6 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://doi.org/10.1038/s41564-025-02085-6) Of the multiple arenaviruses that cause haemorrhagic fevers in the Americas, all lack reliable therapeutic options, and only one has a vaccine. The arenavirus glycoprotein complex (GPC) binds cellular receptors and mediates pH-dependent fusion of viral... - [ descriptionPublisher's Version](https://doi.org/10.1038/s41564-025-02085-6) 2025. “[Structures of Human Organellar SPFH Protein Complexes](/publication/structures-human-organellar-spfh-protein-complexes-0)”, 16, 1, Pp. 10064+. doi:10.1038/s41467-025-65078-3 2025. “[Structures of Human Organellar SPFH Protein Complexes](/publication/structures-human-organellar-spfh-protein-complexes-0)”, 16, 1, Pp. 10064+. doi:10.1038/s41467-025-65078-3 - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://doi.org/10.1038/s41467-025-65078-3) Stomatin, Prohibitin, Flotillin, and HflK/C (SPFH) family proteins are found in all kingdoms of life and in multiple eukaryotic organelles. SPFH proteins assemble into homo- or hetero-oligomeric rings that form domed structures. Most SPFH assemblies also... - [ descriptionPublisher's Version](https://doi.org/10.1038/s41467-025-65078-3) 2025. “[Translational Activators Align MRNAs at the Small Mitoribosomal Subunit for Translation Initiation](/publication/translational-activators-align-mrnas-small-mitoribosomal-subunit-translation-initiation)”. doi:10.1038/s41594-025-01726-y 2025. “[Translational Activators Align MRNAs at the Small Mitoribosomal Subunit for Translation Initiation](/publication/translational-activators-align-mrnas-small-mitoribosomal-subunit-translation-initiation)”. doi:10.1038/s41594-025-01726-y - add\_circle do\_not\_disturb\_on Abstract - [ descriptionPublisher's Version](https://doi.org/10.1038/s41594-025-01726-y) Mitochondrial gene expression is essential for oxidative phosphorylation. Mitochondrial-encoded mRNAs are translated by dedicated mitochondrial ribosomes (mitoribosomes), whose regulation remains elusive. In Saccharomyces cerevisiae, nuclear-encoded... - [ descriptionPublisher's Version](https://doi.org/10.1038/s41594-025-01726-y) [ More arrow\_circle\_right ](/publications) [ More arrow\_circle\_right ](/calendar)