A novel mass spectrometry cluster for high-throughput quantitative proteomics

Magnus Palmblad, Yuri E.M. van der Burgt, Ekaterina Mostovenko, Hans Dalebout, André M. Deelder

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


We have developed and implemented a novel mass spectrometry (MS) platform combining the advantages of high mass accuracy and resolving power of Fourier transform ion cyclotron resonance (FTICR) with the economy and speed of multiple ion traps for tandem mass spectrometry. The instruments are integrated using novel algorithms and software and work in concert as one system. Using chromatographic time compression, a single expensive FTICR mass spectrometer can match the throughput of multiple relatively inexpensive ion trap instruments. Liquid chromatography (LC)-mass spectrometry data from the two types of spectrometers are aligned and combined to hybrid datasets, from which peptides are identified using accurate mass from the FTICR data and tandem mass spectra from the ion trap data. In addition, the high resolving power and dynamic range of a 12 tesla FTICR also allows precise label-free quantitation. Using two ion traps in parallel with one LC allows simultaneous MS/MS experiments and optimal application of collision induced dissociation and electron-transfer dissociation throughout the chromatographic separation for increased proteome coverage, characterization of post-translational modifications and/or simultaneous measurement in positive and negative ionization mode. An FTICR-ion trap cluster can achieve similar performance and sample throughput as multiple hybrid ion trap-FTICR instruments, but at a lower cost. We here describe the first such FTICR-ion trap cluster, its performance and the idea of chromatographic compression.

Original languageEnglish (US)
Pages (from-to)1002-1011
Number of pages10
JournalJournal of the American Society for Mass Spectrometry
Issue number6
StatePublished - Jun 2010
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Spectroscopy


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