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.
|Close, William; Neumann, Matthias; Schmidt, Andreas et al. (2018) Physical basis of amyloid fibril polymorphism. Nat Commun 9:699|
|Loveland, Anna B; Demo, Gabriel; Grigorieff, Nikolaus et al. (2017) Ensemble cryo-EM elucidates the mechanism of translation fidelity. Nature 546:113-117|
|Liu, Yuhang; Pan, Junhua; Jenni, Simon et al. (2017) CryoEM Structure of an Influenza Virus Receptor-Binding Site Antibody-Antigen Interface. J Mol Biol 429:1829-1839|
|Abeyrathne, Priyanka D; Koh, Cha San; Grant, Timothy et al. (2016) Ensemble cryo-EM uncovers inchworm-like translocation of a viral IRES through the ribosome. Elife 5:|
|Schmidt, Andreas; Annamalai, Karthikeyan; Schmidt, Matthias et al. (2016) Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril. Proc Natl Acad Sci U S A 113:6200-5|
|Chou, Hui-Ting; Dukovski, Danijela; Chambers, Melissa G et al. (2016) CATCHR, HOPS and CORVET tethering complexes share a similar architecture. Nat Struct Mol Biol 23:761-3|
|Dimitrova, Yoana N; Jenni, Simon; Valverde, Roberto et al. (2016) Structure of the MIND Complex Defines a Regulatory Focus for Yeast Kinetochore Assembly. Cell 167:1014-1027.e12|
|van der Feltz, Clarisse; Pomeranz Krummel, Daniel (2016) Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method. J Vis Exp :|
|Loveland, Anna B; Bah, Eugene; Madireddy, Rohini et al. (2016) Ribosome•RelA structures reveal the mechanism of stringent response activation. Elife 5:|
|Baytshtok, Vladimir; Fei, Xue; Grant, Robert A et al. (2016) A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure 24:1766-1777|
Showing the most recent 10 out of 152 publications