The EM Core of this Program Project has two related purposes - to support instrumentation essential for the research proposed in the four projects of this grant and to facilitate application of the methods being developed in these projects to collaborative and independent efforts at Harvard Medical School (HMS), Brandeis, and elsewhere. The Core is a single entity with two locations ~ one at HMS (designated Core A) and one at Brandeis (designated Core B) ~ and members of all laboratories have access, when suitably trained, to instruments at either institution. By providing EM and computational facilities, the core allows the Pis of these projects to collaborate with each other and with groups in and outside of the HMS and Brandeis communities and to train postdoctoral fellows and students in the relevant methods. The principal component of the HMS core (Core A) is the electron microscopy facility, which houses four FEI electron microscopes: a Polara, a Tecnai F20, a Tecnai T12, and a CM 10. The Polara and two Tecnai microscopes are equipped with cryo-stages. The core supports the operation of these microscopes and necessary ancillary equipment as well as the salary of an EM technician who supports the facilities manager. The core also has a computational component that maintains and upgrades all standard EM software, including program suites such as FREALIGN, IMAGIC, and SPIDER, through a structural biology computational grid (SBGrid) established by the Center for Molecular and Cellular Dynamics at HMS.
Detailed 3D images of large macromolecular complexes inform us about underlying mechanisms of their function in cells. The Core will enable electron cryo-microscopy for 3D visualization at high resolution and promote the development of new techniques to obtain and process image data from samples containing a mixture of different complexes and states.
|Tran, Timothy H; Hsiao, Yu-Shan; Jo, Jeanyoung et al. (2015) Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase. Nature 518:120-4|
|Luque, Daniel; Gómez-Blanco, Josué; Garriga, Damiá et al. (2014) Cryo-EM near-atomic structure of a dsRNA fungal virus shows ancient structural motifs preserved in the dsRNA viral lineage. Proc Natl Acad Sci U S A 111:7641-6|
|Rohou, Alexis; Grigorieff, Nikolaus (2014) Frealix: model-based refinement of helical filament structures from electron micrographs. J Struct Biol 186:234-44|
|Svidritskiy, Egor; Brilot, Axel F; Koh, Cha San et al. (2014) Structures of yeast 80S ribosome-tRNA complexes in the rotated and nonrotated conformations. Structure 22:1210-8|
|Szyk, Agnieszka; Deaconescu, Alexandra M; Spector, Jeffrey et al. (2014) Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase. Cell 157:1405-15|
|Anthony, Kelsey C; You, Changjiang; Piehler, Jacob et al. (2014) High-affinity gold nanoparticle pin to label and localize histidine-tagged protein in macromolecular assemblies. Structure 22:628-35|
|Bigalke, Janna M; Heuser, Thomas; Nicastro, Daniela et al. (2014) Membrane deformation and scission by the HSV-1 nuclear egress complex. Nat Commun 5:4131|
|Kuang, Yi; Long, Marcus J C; Zhou, Jie et al. (2014) Prion-like nanofibrils of small molecules (PriSM) selectively inhibit cancer cells by impeding cytoskeleton dynamics. J Biol Chem 289:29208-18|
|Koh, Cha San; Brilot, Axel F; Grigorieff, Nikolaus et al. (2014) Taura syndrome virus IRES initiates translation by binding its tRNA-mRNA-like structural element in the ribosomal decoding center. Proc Natl Acad Sci U S A 111:9139-44|
|Eisele, Dörthe M; Arias, Dylan H; Fu, Xiaofeng et al. (2014) Robust excitons inhabit soft supramolecular nanotubes. Proc Natl Acad Sci U S A 111:E3367-75|
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