Mass Spectrometry Lab – E130 BNSN

LTQ OrbiTrap-XL +ETD - This instrument excels at high-throughput proteomic, lipidomic and metabolomic analysis. Up front, state-of-the-art chromatographic sample separation is performed on an Eksigent nanoLC-Ultra2D splitless low-flow UPLC that allows for the use of ultra high pressures across capillary columns packed with micro particles (1.5-1.7um). Two 10-port valves can be plumbed for multiple 2-dimensional chromatographic separation strategies. Bridging the chromatography and the mass spectrometer is a sensitive nano-electrospray source (10um ID tip). The instrument itself can be thought of as three mass spectrometers working in concert. The linear ion trap (LTQ) ushers packets of ions into the orbitrap and performs collision induced dissociation (CID) on a near infinite series of ion fragments (MSn) besides serving as a high speed mass analyzer when needed. Using flouranthene free-radical-ions generated in the backend GC-MS, the LTQ can also perform electron transfer dissociation (ETD) which can be used to 1) fragment larger, higher charge state ions and 2) to gently fragment peptides with post-translational modifications (PTMs) in order to determine exact PTM location. The orbitrap is the first fundamentally new mass analyzer in 30 years and yields near FTICR mass accuracy (0.5-2 ppm) and resolution but without the need for a superconducting magnet. Within a fairly broad range, its mass accuracy is sufficient to identify an analyte's atomic composition from its precursor mass alone. A high collision cell near the orbitrap gives the instrument a total of three different strategies for fragmenting ions to ensure confident identification. Altogether, (with less than 1% error in peptide identifications) over 2300 proteins from a HEK293 cell lysate can be identified in 2.5 hours of analysis- nearly 1000 proteins/hour.

9.4 Tesla FTICR /MS (Fourier Transform Ion Cyclotron Resonance Mass Spectrometer) - This instrument, which was installed in 2010, is the new champion in the Intermountain West. It has twice the mass resolving power, twice the quadrupolar axialization efficiency, twice the data acquisition speed, and twice the upper mass limit of the 4.7 Tesla instrument. It also has 4 times better maximum ion kinetic energy, ion trapping capacity, ion trapping duration, and signal-to-noise. This mass spectrometer is equipped with two data acquistion systems, a "stock" console from the manufacturer, Bruker Daltonics, and a custom-built, state-of-the-art system designed at the National High Magnetic Field Laboratory at Florida State University. It is used for research and teaching purposes within the department. The primary research applications on this instrument involve characterization of supramolecular structures as described above for the 4.7 Tesla system, but the experiments can be done more quickly and more accurately with this instrument's larger superconducting magnet. The 9.4 Tesla instrument is particularly valuable for applications that require ultra-high mass resolving power, such as the complex mixtures of compounds typical of biological samples. Resolving powers in excess of one million are routinely achieved, along with mass measuring accuracy of better than one part per million; at this level of accuracy, simply measuring the mass is often sufficient to determine molecular formulas. BYU undergraduate students have access to this state-of-the-art instrument in physical chemistry and instrumental analysis lab courses, while graduate students use it to further their research projects.