Search

Harvard Cryo-EM Center helps researchers transform biomedical research, one structure at a time

News

"Researchers around the world have embraced cryo-EM for its enhanced power and for the myriad possibilities it offers to advance the rational design and evaluation of therapies. In recognition of the importance of this technology to the future of...

Citations and Acknowledgments

Page

After each data collection, staff will provide a summary of optics and software parameters used on each specific instrument. Please acknowledge the support of The Harvard Cryo-EM Center for Structural Biology in research publications arising from use of...

A New Era: Inaugural symposium lauds Harvard’s new cryo-EM center for structural biology

News

To celebrate the new Harvard Cryo-EM Center for Strucutral Biology, HMS hosted the Inagural Symposium on May 30. The day-long event featured some of the world’s most esteemed structural biologists, including two Nobel laureates. Reflecting Harvard’s...

Cryo-EM Center Policies

Page

Updated September 16, 2022 The Harvard Cryo-EM Center for Structural Biology is a collaboration among Harvard University, Dana-Farber Cancer Institute, Boston Children’s Hospital, and Massachusetts General Hospital. The facility, housed on the Harvard...

The eRF1 degrader SRI-41315 acts as a molecular glue at the ribosomal decoding center

Journal Article

Translation termination is an essential cellular process, which is also of therapeutic interest for diseases that manifest from premature stop codons. In eukaryotes, translation termination requires eRF1, which recognizes stop codons, catalyzes the...

Sub-3-Å cryo-EM structure of RNA enabled by engineered homomeric self-assembly

Journal Article

High-resolution structural studies are essential for understanding the folding and function of diverse RNAs. Herein, we present a nanoarchitectural engineering strategy for efficient structural determination of RNA-only structures using single-particle...

Formation of thyroid hormone revealed by a cryo-EM structure of native bovine thyroglobulin

Journal Article

Thyroid hormones are essential regulators of metabolism, development, and growth. They are formed from pairs of iodinated tyrosine residues within the precursor thyroglobulin (TG), a 660-kDa homodimer of the thyroid gland, by an oxidative coupling...

Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane

Journal Article

The entry of SARS-CoV-2 into host cells depends on the refolding of the virus-encoded spike protein from a prefusion conformation, which is metastable after cleavage, to a lower-energy stable postfusion conformation1,2. This transition overcomes kinetic...

Cryo-EM Structure of Recombinantly Expressed hUGDH Unveils a Hidden, Alternative Allosteric Inhibitor

Journal Article

De novo identification of mammalian ciliary motility proteins using cryo-EM

Journal Article

Cryo-EM structure of a RAS/RAF recruitment complex

Journal Article

RAF-family kinases are activated by recruitment to the plasma membrane by GTP-bound RAS, whereupon they initiate signaling through the MAP kinase cascade. Prior structural studies of KRAS with RAF have focused on the isolated RAS-binding and cysteine-rich...

Cryo-EM structure of an activated GPCR–G protein complex in lipid nanodiscs

Journal Article

G-protein-coupled receptors (GPCRs) are the largest superfamily of transmembrane proteins and the targets of over 30% of currently marketed pharmaceuticals. Although several structures have been solved for GPCR–G protein complexes, few are in a lipid...