Mass Spectrometry Facility Department of Chemistry and Biochemistry University of Texas at Austin
How to download your Open Access data Services Self-service Analysis Chemical and Biological Analysis Proteomics Protocols (PDF) Equipment People Location Costs Operating Policies Chemical Analysis Form (PDF) Biological/Proteomics Form (PDF) Self-service Rule (PDF)
Services: 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: Routine chemical and biological sample analysis, The training of students and postdoctoral associates to run the self-service equipment, 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. Self-service Analysis Open-Access LC-MS/MS Self-service GC-MS/MS Self-service MALDI-MS Proteins sequence database search Chemical and Biological Analysis Low- and high-resolution mass spectrometry of moderately pure organic and inorganic compounds using EI, CI (in conjunction with direct exposure and direct insertion probes), FAB, ESI, and MALDI. Analysis of organic or biological mixtures by GC-MS or HPLC-MS. Analysis of intact proteins and oligonucleotides to provide molecular weight information. Proteomics Protein identification by mass spectrometry from gel or solution phases. This include, gel destaining, solution phase reduction/alkylation, enzymatic digestion, MALDI or ESI-MS peptide mapping, LC-MS/MS peptide sequencing, protein sequence database searching. Characterization protein post-translational modifications (e.g., phosphorylation, etc.), protein expression profiling, and direct analysis by ESI-MS of protein interactions with ligands and other proteins. Whole cell, or sub-celluar proteomics using 2D-LC MALDI-MS/MS or 2D-LC ESI-MS/MS. Please consult Rambod Daneshfar for complicated sample analysis, or for projects such as intact protein or oligonucleotide analysis, quantitative analysis, proteomics, post translational modifications, etc. Because the success of these analyses is largely depends on sample preparation, it is strongly recommended researchers to follow our Sample Preparation Protocols. Equipment: 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. People The Members of MSF include: Dr. Karin Keller, Dr. Rambod Daneshfar, Dr. Ian Riddington, and Aaron Rogers. Location: The MSF is located in the 1.4 corridor of the Welch Hall. The sample submission desk is located outside of Welch 1.402. Address for samples submitted by mail: Mass Spectrometry Department of Chemistry and Biochemistry 1 University Station A5300 The University of Texas at Austin Austin, Texas 78712 Tel: 512-471-7344 Costs: Charges are per sample, per ionization mode for low-resolution analysis; and per sample, per ionization mode, per peak for the high resolution analysis. Operating Policies: Each sample should be accompanied by the appropriate sample submission form Chemical analysis submission form (PDF) Biological protemics analysis submission form (PDF) 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 the Self-service Operation Rules PDF document for additional information. Training classes usually run about 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.