• Nuclear Magnetic Resonance (NMR)

  • Mass Spectrometry: The facility has state-of the art instrumentation that can be used either directly by users or by facility staff for the analysis of biological samples.

  • Cryo-electron microscopy (cryoEM) is an essential structural biology tool that enables determination of three-dimensional (3D) structures of large biological macromolecules, macromolecular complexes, and cell components of biomedical interest, bridging the gap between the complementary tools of X-ray crystallography, nuclear magnetic resonance spectroscopy (NMR) and visible light microscopy imaging.

    Recent advances in cryoEM have made it possible to visualize extremely complex systems, thereby enhancing our understanding of biology and human disease at the molecular level. The rapid growth in the field of cryoEM is reflected by dramatic increases in the pace of structure depositions to the Protein Databank and EMDB.  The diversity of cryoEM structure determination targets has also exploded to include macromolecular machines essential for protein synthesis, folding, degradation, energy generation and motile force; large, multicomponent viruses, such as Zika virus; and complexes of viruses with host cell components.

    Now even the caveat that a protein or a macromolecular machine might be too small for cryoEM is no longer a major concern. A structure of hemoglobin at 3.4 Å resolution was recently presented at the FEI New York city CryoEM Symposium. The structure was obtained using the same phase plate technology available in our facility.