Mass Spectrometry Resource

Our Mission

The NIH/NIGMS-supported biomedical mass spectrometry (MS) research resource develops novel MS-based solutions to analytical challenges, and provides service, collaboration, and training for MS-based characterization, identification and quantification of all biomolecular classes extracted from in vitro and in vivo model systems. The MS research resource supports integrated research programs in ion chemistry, protein biophysics, targeted and untargeted proteomics, lipidomics, metabolomics, and stable isotope labeled biomolecules focused on advancing MS platforms, software and their analytical capabilities for expanding biological knowledge, and training the next generation of translational scientists interested in biomedical applications of MS.

Our Goals

  • Establish collaborative research projects with basic and applied investigators at Washington University and other institutions
  • Develop novel and provide routine mass spectrometry-based analytical services
  • Educate and train students/fellows/junior faculty in the use and applications of mass spectrometry
  • Disseminate our research findings and inform the community about biomedical mass spectrometry

Services

Academic users receive a subsidized rate for services. For industrial and governmental scientists, the MS resource also offers capabilities and services that cannot be obtained from commercial laboratories owing to lack of equipment, capabilities, or expertise. These services are provided on an unsubsidized fee-for-service basis. Industrial and government scientists are requested to contact commercial laboratories before considering service at the MS resource.

If you publish or share data that utilizes our mass spectrometry services, be sure to acknowledge our support. For example, please include the following sentence or something similar: “This study made use of the NIH/NIGMS Biomedical Mass Spectrometry Resource at Washington University in St. Louis, MO, which is supported in part by the National Institute of General Medical Science within the National Institutes of Health through 5P41GM103422.” In addition, publications that result from work carried out on instruments or aided by personnel that receive support from the MS resource grant must comply with the NIH Public Access Policy.

Ready to get started? View our fee schedule or complete an MS sample analysis form.

If you are not sure about what type of analysis will meet your needs, please consult our "Instrumentation and Ionization Methods" tutorial or contact Henry Rohrs.

Service Location
Low-resolution EI, CI, GC-MS, and LC-MS Danforth, Medical School
 ESI MS Danforth, Medical School
MALDI Danforth, Medical School
High-resolution MALDI and GC-MS Danforth
Isotope ratio MS Medical School
Accurate mass FTMS Danforth, Medical School
High-resolution FTICR: Intact mass measurement and tandem MS Danforth
Tandem MS: SRM, MRM Medical School
Tandem MS: Bottom-up proteomics Danforth, Medical School
Tandem MS: Top-down proteomics Danforth
H/D exchange MS Danforth
MS data analysis: Lipids (LipidQA) Danforth, Medical School
MS data analysis: Proteins (Mascot, PD) Danforth, Medical School
MS data analysis: Metabolites (Mass Profiler Professional, METLIN, Fiehn, NIST) Danforth, Medical School

Personnel

Michael L. Gross

​Professor of Chemistry and of Immunology and Internal Medicine (School of Medicine)

Professor Gross's main research goal is the development of biophysical methods that use mass spectrometry to understand proteins, their interfaces, solvent accessibility, affinities of binding, and their folding and unfolding.

Henry Rohrs

Instrumentation Specialist, NIH NCRR Biomedical Mass Spectrometry Facility

Rohr's research focuses on biological mass spectrometry, FTICR instrument development, and proteomics.

Learn More

Looking for tutorials or other additional details about the mass spectrometry resource?

Shared Resources