Acquisition of a Thermo Fisher Scientific Q Exactive UHMR mass spectrometer

Project: Research project

Description

The acquisition of a Q Exactive UHMR instrument will enable Northwestern’s Proteomics core to offer new service lines that will bring leading edge native mass spectrometric techniques into conversation with truly transformative biological questions. The Proteomics Core, now in its 8th year, is a well-established resource that supports hundreds of researchers in both the basic science and clinical/translational realms. While the current instruments and service lines offered by the core are capable of answering many of these researcher’s questions, the Core has a major deficit in structural proteomics. The high m/z range of the Q Exactive UHMR will enable structural mass spectrometric studies on proteins and protein complexes ranging from 100 kDa to 5 MDa, making it possible to answer questions regarding composition, stoichiometry, metal/co-factor binding and more. Major projects include mechanistic studies of the nitrogenase enzyme, stoichiometric studies of metalloproteins such as methane monooxygenase, dynamic studies of ribosomes and compositional studies of telomerase and CRISPR/Cas9. Further, applications for minor users range from the analysis of nanoparticles to complexes of a therapeutic antibody with aβ oligomers in Alzheimer’s research. To support the acquisition and development of these service lines, the University has committed to offsetting costs during the first two years of operation by supporting a research professional at 50% effort. The University also provides operational and fiscal management teams as well as infrastructure. The acquisition of the Q Exactive UHMR will lead to a real and lasting impact on current and future NIH supported research across a broad range of topics that are vital to human health and wellness.
StatusActive
Effective start/end date4/1/183/31/20

Funding

  • Office of the Director, National Institutes of Health (1S10OD025194-01)

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Mass spectrometers
methane monooxygenase
Clustered Regularly Interspaced Short Palindromic Repeats
Metalloproteins
Nitrogenase
Telomerase
Oligomers
Stoichiometry
Proteins
Metals
Health
Nanoparticles
Antibodies
Enzymes
Chemical analysis
Proteomics
Costs