mass spec page

The Mass Spectrometry Facility (MSF) of the Department of Chemistry and Biochemistry/Institute for Cellular and Molecular Biology is a state-of-the-art facility that provides services to a large number of researchers. The facility provides: 1) Routine chemical and biological sample analysis, 2) training of students and postdoctoral associates to run the self-service equipment, 3) independent and collaborative research in mass spectrometry.

The MSF serves the MS needs of a large number of scientists not only in the College of Natural Sciences but other colleges such as Pharmacy, Biological Sciences, Engineering, etc. In addition to UT campus, The MSF has provided services to other academic institutions when the expertise for special analysis was not available at these institutions. The services provided by the MSF divide into two general categories of chemical and biological analysis. In the chemical area, the MSF is capable of analyzing gas, liquid, and solids in pure or complex mixture forms. Chemical analysis can be performed both at low and high resolution. High-resolution analysis provides chemical composition information. In the area of biochemical analysis, the MSF is capable of analyzing amino acids, peptides, proteins, oligonucleotides, etc.; however, protein identification is the most common form of analysis in this area. Analyses of chemical and biological samples are performed utilizing a variety of sample introduction, separation, and ionization techniques.

The MSF is equipped with a variety of mass spectrometers including: 1) A triple quadrupole mass spectrometer equipped with convention ionization techniques (EI, CI, and FAB) in conjunction with direct exposure and direct insertion probes, and GC sample introduction techniques. This mass spectrometer can analyze compounds with m/z of up to 4000 in both positive and negative ionization modes. 2) A high-resolution magnetic sector instrument equipped with EI, CI, FAB, and positive/negative ionization modes. 3) A self-services GC-MS/MS, capable of analyzing low molecular (<1000 Da), high vapor pressure compounds utilizing EI, or CI in positive or negative ionization modes. This instrument is equipped with an auto-sampler for automated sample analysis. 4) An Open Access HPLC-/MS/MS with m/z range of up to 4000, and 5) a self-service linear MALDI-TOF MS. In addition, recently several state of the art mass spectrometers and their ancillary equipment (1D and 2D nano-LC) have been purchased using funds from NIH, NSF. These include: 6) an ESI/MALDI Q-TOF MS (with m/z range of 8000 for the front end quadrupole), and 8) two high field (9.4 and 12 Tesla) Qq-FTICR mass spectrometers equipped with a variety of ionization and dissociation techniques including ESI, MALDI, and CID. Moreover, the facility is equipped with a variety of separation techniques including on-line nano-2D-LC and capillary electrophoresis for sensitive proteomics as well as self-service protein sequence database searching for mass spectrometry-based protein identification using Mascot and Sequest.

Each sample should be accompanied by a sample submission form (chemical analysis here or biological protemics analysis here) and each sample vial should have a sample submission tag attached to the vial (and not to the cap). HPLC and ESI samples should be submitted in screw-cap or crimp top vials.

Self-service operation can only be performed by those who have been trained by the MSF staff members in charge of the self-service instruments (see Self-service Operation Rules). Training classes are usually ~an hour. Researchers interested in self-service operation should register for the courses in Welch 1. 406.

Protein and peptide molecular weights can be measured on a few picomole or less of material, with accuracies of 0.1% by MALDI and 0.03% by ESI, respectively, on the Voyger and LCQ instruments and less on the Q-TOF, and FTMS instruments.

Samples are run based on first-come first serve policy.