BILLERICA, Mass.–Bruker Daltonics announced today that the laboratory of Professor Michael Gross at Washington University in St. Louis has ordered a package consisting of a Bruker 12 Tesla FTMS and a maXis UHR-TOF, primarily for applications in top-down proteomics in close collaboration with Professor Reid Townsend, who heads proteomics efforts at Washington University. The researchers also plan to use the maXis for other important applications including accurate mass formula determination of small molecules and protein structure studies that employ their unique methods called PLIMSTEX, SIMSTEX, and FPOP (OH radical footprinting).

In top-down proteomics, intact proteins are first measured to determine their molecular weights, then selected proteins are fragmented in the gas phase, and the fragments are again measured with the ultra-high resolution and mass accuracy of FTMS. The latest Bruker ESI-Qq-FTMS with a high field 12 Tesla magnet features a mass resolving power of two million (2,000,000 FWHM) and is a superb tool for analyzing very complex spectra in top-down proteomics. By correlating the expected weights of the fragments from the protein sequence with the experimental results, the location of important protein post-translational modifications (PTMs) such as phosphorylation or glycosylation can be unambiguously determined. This functionally important information about protein modifications is often lost in more traditional bottom-up proteomics.

The Bruker FTMS provides not only the highest mass resolving power and mass accuracy available on any mass spectrometer for such measurements, but also offers the most versatile suite of tools for fragmenting the proteins. Besides the novel Continuous Accumulation of Selected Ions (CASI™) which allows researchers to enrich selectively the signal from a selected protein or one of its large multiply charged fragments, the Bruker FTMS already includes external collision-cell or internal ICR cell Collision Induced Dissociation (CID), as well as Electron Capture Dissociation (ECD) in the ICR cell. Critical to the top-down analysis process are also software tools that eliminate tedious manual data interpretation, such as the unique Bruker SNAP ™ algorithm.

Furthermore, an agreement between Bruker and the laboratory of Prof. Gross gives his lab early access to the unique, newly developed front-end Electron Transfer Dissociation (ETD) module for FTMS, a new, sensitive and easy-to-use method for fragmenting peptides and proteins in a fast non-ergodic process that again preserves PTMs. Bruker is the world-leader in ETD on its HCT high-capacity ion traps, and has now made this sensitive ETD capability available also on its ultra-high resolution ESI-FTMS systems as a work-in-progress research capability.

Dr. Michael Gross, a professor in the departments of chemistry, immunology and medicine, and the Editor of the Journal of the American Society for Mass Spectrometry, commented: “We and our collaborators at the Washington University Medical School have many scientific questions that can best be addressed by top-down proteomics. The number and nature of protein modifications are critically important in understanding protein function. We are excited to be working with Bruker Daltonics on their high-field FTMS for top-down proteomics, using the unique combination of existing CID and in-cell ECD tools, as well as on the further development and applications of the new front-end ETD capability. We expect the acquisition of this instrument to help us solve biologically and medically important problems using the top-down approach, and it will put us in a leadership position in the applications of top-down proteomics.”

The new Bruker ultra-high resolution time-of-flight (UHR-TOF) mass spectrometer maXis is the first and only instrument available today that enables the previously incompatible trends in modern mass spectrometry of ultra-high mass resolution and very fast UHPLC chromatographic separations. Exceptional mass accuracy of better than 1 ppm in MS and MS/MS mode, ultra-high mass resolving power of 40,000 to 60,000 at up to 20 Hz, dynamic range over 5 orders of magnitude, high m/z capabilities, exceptional stability allowing 1.5 mDa high-resolution extracted ion chromatograms, as well as outstanding sensitivity are all maintained simultaneously even when coupled to the fastest available chromatography separation systems, delivering a powerful mass spectrometer for a broad range of life-science applications. maXis has already been proven as an exceptional tool in quantitative proteomics, peptide and intact protein analysis, but also for rapid small molecule identification using the unique SmartFormula™ 3D method for on-the-fly unambiguous molecular formula read-out, co-developed with Pfizer, UK.

“We are delighted that Professor Gross, who has an outstanding record in the development of mass spectrometry for new applications, has chosen Bruker Daltonics as a partner in developing applications in top-down proteomics,” commented Dr. Gary Kruppa, Bruker Daltonics’ Vice President for Business Development. “We view our ESI-FTMS with high field magnets as the ultimate platform for top-down proteomics and are pleased to collaborate with Professor Gross in this field. The maXis as a high-throughput, high-performance research tool for applications in proteomics and small molecule research, and the collaboration on the development of front-end ETD, make this a very exciting and important research collaboration for Bruker.”

Professor Gross observed further: “The maXis will have many applications in our laboratory. The ultra-high resolution of this instrument will allow us to do experiments we have developed in our lab such as PLIMSTEX, SIMSTEX, and other protein mapping strategies at high speed with isotopic resolution of proteins up to 40 kDa. We are very excited about applying the maXis to this work, but we also see that the maXis will be a superb instrument for the more routine work done in our facility, such as confirmation of small synthetic molecules important in chemistry and metabolomics by using accurate mass MS and MS/MS. We are pleased about bringing new tools such as SmartFormula™ 3D to our facility and making them available to our collaborators and clients.”