Ultra high resolution linear ion trap Orbitrap mass spectrometer (Orbitrap Elite) facilitates top down LC MS/MS and versatile peptide fragmentation modes
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Although only a few years old, the combination of a linear ion trap with an Orbitrap analyzer has become one of the standard mass spectrometers to characterize proteins and proteomes. Here we describe a novel version of this instrument family, the Orbitrap Elite, which is improved in three main areas. The ion transfer optics has an ion path that blocks the line of sight to achieve more robust operation. The tandem MS acquisition speed of the dual cell linear ion trap now exceeds 12 Hz. Most importantly, the resolving power of the Orbitrap analyzer has been increased twofold for the same transient length by employing a compact, high-field Orbitrap analyzer that almost doubles the observed frequencies. An enhanced Fourier Transform algorithm-incorporating phase information-further doubles the resolving power to 240,000 at m/z 400 for a 768 ms transient. For top-down experiments, we combine a survey scan with a selected ion monitoring scan of the charge state of the protein to be fragmented and with several HCD microscans. Despite the 120,000 resolving power for SIM and HCD scans, the total cycle time is within several seconds and therefore suitable for liquid chromatography tandem MS. For bottom-up proteomics, we combined survey scans at 240,000 resolving power with data-dependent collision-induced dissociation of the 20 most abundant precursors in a total cycle time of 2.5 s-increasing protein identifications in complex mixtures by about 30%. The speed of the Orbitrap Elite furthermore allows scan modes in which complementary dissociation mechanisms are routinely obtained of all fragmented peptides.
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Recent advances in mass spectrometer hardware have provided a boost in depth of standard analyses and enabled near-complete model proteome quantification in minimal measuring time.
“Recent advances in mass spectrometer hardware (76, 77) have provided a boost in the depth of standard analyses and enabled near-complete model proteome quantification in minimal measuring time (6).”
From Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ (2014) · cites this paper as [76]
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- Authors
- Michalski, A., Damoc, E., Lange, O., Denisov, E., Nolting, D., Müller, M., Viner, R., Schwartz, J., Remes, P., Belford, M., Dunyach, J.-J., Cox, J., Horning, S., Mann, M., & Makarov, A.
- Affiliations
- Max Planck Institute of Biochemistry (DE)
- Thermo Fisher Scientific (Germany) (DE)
- Thermo Fisher Scientific (United States) (US)
- Corresponding author
- Mann, Matthias
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 11
- Issue
- 3
- Pages
- O111.013698
- ISSN
- 1535-9476 (ISSN-L)
- PMC
- PMC3316736
- OpenAlex
- W2066928228
- Cited by
- 373
- References
- 41
- Citations by year
- 2026: 7 · 2025: 11 · 2024: 17 · 2023: 15 · 2022: 16 · 2021: 22 · 2020: 21 · 2019: 24 · 2018: 19 · 2017: 32 · 2016: 20 · 2015: 35 · 2014: 41 · 2013: 62 · 2012: 29
- FWCI
- 19.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular & Cellular Proteomics (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Funders
- Northwestern University
- European Commission (201648)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Keywords
- linear ion trap, top-down proteomics, peptide fragmentation, resolving power, Fourier transform algorithm, shotgun proteomics
- MeSH terms
- Chromatography, Liquid, HeLa Cells, Humans, Peptide Fragments, Proteome, Proteomics, Tandem Mass Spectrometry
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