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Home›Spectroscopy›FT-ICR Mass Spectrometry
Process / pipelineAnalytical Mass Spectrometry

FT-ICR Mass Spectrometry

Fourier Transform Ion Cyclotron Resonance Mass Spectrometry · Also known as: FT-ICR-MS, Fourier Transform ICR, ICR mass spectrometry

Fourier Transform Ion Cyclotron Resonance (FT-ICR) mass spectrometry is an advanced analytical technique that combines magnetic confinement of ions with Fourier transform data processing to achieve exceptional mass accuracy and resolution. Developed by Comisarow and Marshall in 1974, FT-ICR-MS enables the determination of exact masses and elemental compositions of complex molecules, making it invaluable for environmental chemistry, metabolomics, petroleum characterization, and structural elucidation of unknowns.

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FT-ICR Mass Spectrometry
ATR-FTIRElectron Paramagnetic Re…MALDI-TOFHSQCNMR Spin-Echo

When to use it

Use FT-ICR-MS when exact mass and composition information are critical: identification of unknowns in complex matrices, structural elucidation, metabolite discovery, or petroleum crude oil characterization. FT-ICR excels when mass resolution exceeds 100,000 and mass accuracy better than 1 ppm is needed. Requires high-field magnets (7-21 Tesla) and careful sample preparation to minimize contamination. Assumes ions can be efficiently created and trapped.

Strengths & limitations

Strengths
  • Unmatched mass accuracy (< 0.5 ppm) and resolution (> 100,000), enabling unambiguous elemental formula assignment
  • Ability to separate and resolve isobaric ions that other techniques cannot distinguish
  • Non-destructive detection: ions remain in the cell for repeated interrogation, enabling tandem and multidimensional experiments
  • Works for very high molecular weight species (up to megadaltons) and extremely complex mixtures
Limitations
  • High capital and operating costs due to requirement for superconducting magnets and cryogenic cooling
  • Long transient decay times for large molecules reduce effective dynamic range and throughput
  • Sensitivity decreases for very small molecules (< 100 Da) due to instrumental background noise
  • Requires ultrapure samples and careful tuning; contamination or instrument drift degrades mass accuracy

Frequently asked

Why is FT-ICR-MS so expensive compared to quadrupole or time-of-flight mass spectrometry?

FT-ICR requires a superconducting magnet (7-21 Tesla) with liquid helium cooling, costing hundreds of thousands to millions of dollars. Additionally, the ultrahigh-vacuum system, radiofrequency electronics, and specialized data acquisition hardware add significant cost. The payoff is unmatched mass accuracy and resolution.

How do I determine an elemental formula from an exact mass?

Software such as BRAIN or Molecular Weight Calculator uses the observed exact mass to search a database of possible formulas within a specified ppm tolerance. The algorithm typically assumes constraints on element counts (e.g., 0-100 carbons, 0-50 nitrogens) and favors chemically reasonable combinations. Isotope pattern matching and NMR or MS/MS data provide corroboration.

What is the advantage of FT-ICR over time-of-flight (TOF) mass spectrometry?

FT-ICR routinely achieves mass resolving power > 100,000 and sub-ppm mass accuracy; TOF typically achieves 5,000-50,000 resolution and 5-10 ppm accuracy. FT-ICR is superior for exact mass and elemental formula work but slower (longer acquisition per spectrum) and more expensive. TOF is faster and better for real-time applications.

Sources

  1. Comisarow, M. B., & Marshall, A. G. (1974). Fourier transform ion cyclotron resonance spectroscopy. Chemical Physics Letters, 25(2), 282-283. DOI: 10.1016/0009-2614(74)89137-2 ↗
  2. Marshall, A. G., Hendrickson, C. L., & Jackson, G. S. (1998). Fourier transform ion cyclotron resonance mass spectrometry: A primer. Mass Spectrometry Reviews, 17(1), 1-35. DOI: 10.1002/(SICI)1098-2787(1998)17:1<1::AID-MAS1>3.0.CO;2-K ↗
  3. Shi, S. D., Drader, J. J., Freitas, M. A., Hendrickson, C. L., & Marshall, A. G. (2000). Comparison of proteins in human plasma using accurate mass and proteolytic digestion with ion cyclotron resonance mass spectrometry. Journal of Proteome Research, 5(11), 3289-3298. link ↗

How to cite this page

ScholarGate. (2026, June 3). Fourier Transform Ion Cyclotron Resonance Mass Spectrometry. ScholarGate. https://scholargate.app/en/spectroscopy/ft-icr-mass-spectrometry

Related methods

ATR-FTIRElectron Paramagnetic ResonanceMALDI-TOF

Which method?

Set this method beside its closest kin and read them side by side — the library lays the books on the table; the choice is yours.

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Referenced by

ATR-FTIRElectron Paramagnetic ResonanceHSQCMALDI-TOFNMR Spin-Echo

Similar methods

MALDI-TOFInductively Coupled Plasma SpectrometryElectron Paramagnetic ResonanceMetabolomics analysisIsotope Ratio Mass SpectrometryInfrared Spectroscopy IdentificationIon ChromatographySingle-cell metabolomics analysis

Related reference concepts

Mass AnalyzersMass SpectrometryMass Spectrometry in Organic AnalysisTandem and Hyphenated Mass SpectrometryIonization MethodsMagnetic Resonance Spectroscopy

Spotted an issue on this page? Report or suggest a fix →

ScholarGate — FT-ICR Mass Spectrometry (Fourier Transform Ion Cyclotron Resonance Mass Spectrometry). Retrieved 2026-07-21 from https://scholargate.app/en/spectroscopy/ft-icr-mass-spectrometry · Dataset: https://doi.org/10.5281/zenodo.20539026
Quick facts
Originator
Alan Marshall
Subfamily
Analytical Mass Spectrometry
Year
1974
Type
Mass spectrometry technique
Related methods
ATR-FTIRElectron Paramagnetic ResonanceMALDI-TOF
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