The electron microscopy core will house all the instrumentation needed for the recording of high-resolution images and electron diffraction data. It will operate at two sites one at Brandeis and one at Harvard Medical School. The Brandeis part of the core will contain a 300 kV field- emission source, liquid He cooled electron microscope for the very highest resolution work and for thick specimens. It will also contain three 120 kV instruments, two with liquid N2 cryo stages. The Harvard part of the core will contain a 200 kV field emission source microscope and a 120 kV thermionic gun microscope, both with cryostages. This complement of microscopes will allow investigators and their collaborators at both institutions rapid access to routine microscopy for project development and complementary high-end instruments for high- resolution work. The core will be managed by Linda Melanson (Brandeis) and Yifan Cheng (Harvard Medical School)..

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
5P01GM062580-02
Application #
6588152
Study Section
Special Emphasis Panel (ZRG1)
Project Start
2002-04-01
Project End
2003-03-31
Budget Start
Budget End
Support Year
2
Fiscal Year
2002
Total Cost
Indirect Cost
Name
Brandeis University
Department
Type
DUNS #
616845814
City
Waltham
State
MA
Country
United States
Zip Code
02454
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
Loveland, Anna B; Bah, Eugene; Madireddy, Rohini et al. (2016) Ribosomeā€¢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
Laxmikanthan, Gurunathan; Xu, Chen; Brilot, Axel F et al. (2016) Structure of a Holliday junction complex reveals mechanisms governing a highly regulated DNA transaction. Elife 5:
Ha, Jun Yong; Chou, Hui-Ting; Ungar, Daniel et al. (2016) Molecular architecture of the complete COG tethering complex. Nat Struct Mol Biol 23:758-60
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

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