Abstract

? Core B ? Cryo-Electron Microscopy Core The TBSGC will expand its capabilities in structural biology by incorporating cryo-electron microscopy (cryo-EM) as a means to study the structures of proteins that are either not amenable to crystallography, or importantly when crystallography and cryo-EM can be used to ?combine? component x-ray structures into large macromolecular complexes. Recent advances in single-particle cryo-electron microscopy (cryo-EM) have enabled the structure determination of large macromolecular complexes to atomic resolution. This breakthrough is mostly attributed to the development of the instrumentation needed to acquire better images and the software to more reliably process and validate the results. This is especially true for very large protein complexes, like the ribosome, as well as membrane proteins. The core lab at Texas A&M has state of the art instrumentation and expertise through Dr. Junjie Zhang?s group. Dr. Zhang will use the Texas A&M EM facility which is a fully staffed laboratory for help with administrative aspects and even some of the sample preparation and data collection for core samples.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Program Projects (P01)
Project #
5P01AI095208-07
Application #
9984267
Study Section
Special Emphasis Panel (ZAI1)
Project Start
2012-09-01
Project End
2023-07-31
Budget Start
2020-08-01
Budget End
2021-07-31
Support Year
7
Fiscal Year
2020
Total Cost
Indirect Cost

  Institution

Name
Texas A&M Agrilife Research
Department
Type
DUNS #
847205713
City
College Station
State
TX
Country
United States
Zip Code
77845

  Publications

Rittershaus, Emily S C; Baek, Seung-Hun; Krieger, Inna V et al. (2018) A Lysine Acetyltransferase Contributes to the Metabolic Adaptation to Hypoxia in Mycobacterium tuberculosis. Cell Chem Biol 25:1495-1505.e3
Tuukkanen, Anne T; Freire, Diana; Chan, Sum et al. (2018) Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3, and ESX-5 Type VII Secretion Systems. J Mol Biol :
Pham, Truc V; Murkin, Andrew S; Moynihan, Margaret M et al. (2017) Mechanism-based inactivator of isocitrate lyases 1 and 2 from Mycobacterium tuberculosis. Proc Natl Acad Sci U S A 114:7617-7622
Costa, Diego L; Namasivayam, Sivaranjani; Amaral, Eduardo P et al. (2016) Pharmacological Inhibition of Host Heme Oxygenase-1 Suppresses Mycobacterium tuberculosis Infection In Vivo by a Mechanism Dependent on T Lymphocytes. MBio 7:
Matsui, Toshitaka; Nambu, Shusuke; Goulding, Celia W et al. (2016) Unique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation. Proc Natl Acad Sci U S A 113:3779-84
Olive, Andrew J; Sassetti, Christopher M (2016) Metabolic crosstalk between host and pathogen: sensing, adapting and competing. Nat Rev Microbiol 14:221-34
Balderas, Miriam A; Nguyen, Chinh T Q; Terwilliger, Austen et al. (2016) Progress toward the Development of a NEAT Protein Vaccine for Anthrax Disease. Infect Immun 84:3408-3422
Diaz-Ochoa, Vladimir E; Lam, Diana; Lee, Carlin S et al. (2016) Salmonella Mitigates Oxidative Stress and Thrives in the Inflamed Gut by Evading Calprotectin-Mediated Manganese Sequestration. Cell Host Microbe 19:814-25
Lovewell, Rustin R; Sassetti, Christopher M; VanderVen, Brian C (2016) Chewing the fat: lipid metabolism and homeostasis during M. tuberculosis infection. Curr Opin Microbiol 29:30-6
Cheng, Yu-Shan; Sacchettini, James C (2016) Structural Insights into Mycobacterium tuberculosis Rv2671 Protein as a Dihydrofolate Reductase Functional Analogue Contributing to para-Aminosalicylic Acid Resistance. Biochemistry 55:1107-19

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