Open trapped ion cell geometries for Fourier transform ion cyclotron resonance mass spectrometry

Beu, Steven C.; Laude, David A.

doi:10.1016/0168-1176(92)80006-m

Cited by 124 publications

(74 citation statements)

References 26 publications

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“…fused silica capillary, which had been mechanically ground to a uniform thin-walled tip [20]. The electrosprayed ions were transported into the mass spectrometer through a Chait-style atmosphere-to-vacuum interface [21] and externally accumulated [22] [23] cylindrical cell. The ions were subjected to chirp excitation (72 to 320 kHz at 150 Hz/ s) and direct-mode broadband detection (1 Mword data points).…”

Section: Esi-fticr-msmentioning

confidence: 99%

Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry

Nilsson

Cooper²,

Håkansson³

et al. 2002

J. Am. Soc. Mass Spectrom.

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Borrelia burgdorferi sensu lato is a tick-borne pathogen that causes Lyme disease. The characterization of membrane proteins from this and other pathogens may yield a better understanding of the mechanisms of infection and information useful for vaccine design. Characterization of the highly hydrophobic Borrelia outer membrane component P13 from a mutant (OspA Ϫ OspB Ϫ OspC Ϫ and OspD Ϫ ) strain was undertaken by use of a combination of mass spectrometric methods. In a previous investigation, an electrospray ionization (ESI) mass spectrum of the intact protein provided an average molecular weight that was 20 Da lower than the predicted molecular weight. The mass deviation could be explained by a modification of the N-terminus of the protein such as pyroglutamylation (Ϫ17 Da) in combination with the experimental error of measurement, however more information was required. New structural information for this membrane protein was provided by peptide mapping with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI TOF MS) and sequencing with ESI-quadrupole-TOF tandem MS. ESI Fourier transform ion cyclotron resonance (FT-ICR) MS at 9.4 tesla revealed that the Borrelia membrane protein is not only pyroglutamylated, but also contains an amino acid substitution near the N-terminus. (J Am Soc Mass Spectrom 2002, 13, 295-299)

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Section: Esi-fticr-msmentioning

confidence: 99%

Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry

Nilsson

Cooper²,

Håkansson³

et al. 2002

J. Am. Soc. Mass Spectrom.

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“…A 20 min delay time between the start of the LC method and the start of the spot deposition was used. 21 cylindrical open ICR cell. 22,23 Ions were excited by broadband frequency chirp excitation and detected before a single zero-fill, Gaussian apodization, and Fourier transform.…”

Section: Methodsmentioning

confidence: 99%

Vacuum compatible sample positioning device for matrix assisted laser desorption/ionization Fourier transform ion cyclotron resonance mass spectrometry imaging

Aizikov

Smith

Chargin

et al. 2011

Review of Scientific Instruments

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The high mass accuracy and resolving power of Fourier transform ion cyclotron resonance mass spectrometers (FT-ICR MS) make them ideal mass detectors for mass spectrometry imaging (MSI), promising to provide unmatched molecular resolution capabilities. The intrinsic low tolerance of FT-ICR MS to RF interference, however, along with typically vertical positioning of the sample, and MSI acquisition speed requirements present numerous engineering challenges in creating robotics capable of achieving the spatial resolution to match. This work discusses a two-dimensional positioning stage designed to address these issues. The stage is capable of operating in ∼1 × 10 -8 mbar vacuum. The range of motion is set to 100 mm × 100 mm to accommodate large samples, while the positioning accuracy is demonstrated to be less than 0.4 micron in both directions under vertical load over the entire range. This device was integrated into three different matrix assisted laser desorption/ionization (MALDI) FT-ICR instruments and showed no detectable RF noise. The "oversampling" MALDI-MSI experiments, under which the sample is completely ablated at each position, followed by the target movement of the distance smaller than the laser beam, conducted on the custom-built 7T FT-ICR MS demonstrate the stability and positional accuracy of the stage robotics which delivers high spatial resolution mass spectral images at a fraction of the laser spot diameter.

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“…We have recently demonstrated the feasibility of targeted MS/MS based on the abundance ratios (ARs) of 14 N/ 15 N-labeled peptide pairs using an LC-FTICR platform [6]. In a tryptic peptide mixture of Shewanella oneidensis proteins, we were able to specifically target and identify species that were differentially abundant in suboxic versus aerobic conditions; for several identified proteins, differential abundance was confirmed by alternative techniques [7].…”

mentioning

confidence: 96%

“…Briefly, the mass spectrometer incorporates an ESI source (with the chemically etched tip° [12]),°a°heated°capillary°(160°°C),°an°electrodynamic ion°funnel° [13],°a°collisional°quadrupole°for°ion°focusing (Q 0 ), two selection quadrupoles (Q 1 and Q 2 ), an accumulation quadrupole (Q 3 ), and a transfer quadrupole (Q 4 )°that°leads°to°an°open°cylindrical°ICR°trap° [14].°Q 1 is an RF-only quadrupole with notch ejection capability, which offers "dynamic range expansion applied to mass°spectrometry"°(DREAMS)°capability° [15,°16],°but was used only as an ion guide in this study. Q 2 is a commercial quadrupole mass filter (6 mm rod diameter, Extrel) powered by a commercial RF power supply (150-QC, Extrel, Pittsburgh, PA) working at 880 kHz.…”

Section: Fticr Msmentioning

confidence: 99%

Targeted tandem mass spectrometry for high-throughput comparative proteomics employing NanoLC-FTICR MS with external ion dissociation

Kang

Paša‐Tolić

Smith

2007

J. Am. Soc. Mass Spectrom.

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Targeted tandem mass spectrometry (MS/MS) is an attractive proteomic approach that allows selective identification of peptides exhibiting abundance differences, e.g., between culture conditions and/or diseased states. Herein, we report on a targeted LC-MS/MS capability realized with a hybrid quadrupole-7 tesla Fourier transform ion cyclotron resonance (FTICR) mass spectrometer that provides data-dependent ion selection, accumulation, and dissociation external to the ICR trap, and a control software that directs intelligent MS/MS target selection based on LC elution time and m/z ratio. We show that the continuous on-the-fly alignment of the LC elution time during the targeted LC-MS/MS experiment, combined with the high mass resolution of FTICR MS, is crucial for accurate selection of targets, whereas high mass measurement accuracy MS/MS data facilitate unambiguous peptide identifications. . Despite these efforts, many species remain unidentified with various precursor ion selection methods, particularly when low abundance species co-elute with high abundance species and when sample amounts are limited, making it unfeasible to repeat the experiment many times. However, in many proteomics studies, such as clinical studies when one is looking for significant differences between, e.g., healthy and diseased subjects, the goal is to gain insight into the differences in protein abundances among different conditions/states rather than obtaining a global snapshot of the proteome. An LC-MS/MS method that could target "interesting" species (e.g., differentially abundant peptides) for identification, would be particularly beneficial in this context. Some commercial mass spectrometers offer a rudimentary targeted MS/MS capability, but a more advanced capability is not yet commercially available. For instance, Finnigan (San Jose, CA) linear ion trap based spectrometers (LTQ, LTQ-FT, LTQ-Orbitrap) allow targets to be selected based on the m/z value. However, the elution times cannot be precisely specified, and alignment of the LC elution times between different LC-MS analyses cannot be performed, which is an increasingly important issue as LC flow rates are decreased to improve sensitivity [5].We have recently demonstrated the feasibility of targeted MS/MS based on the abundance ratios (ARs) of 14 N/ 15 N-labeled peptide pairs using an LC-FTICR platform [6]. In a tryptic peptide mixture of Shewanella oneidensis proteins, we were able to specifically target and identify species that were differentially abundant in suboxic versus aerobic conditions; for several identified proteins, differential abundance was confirmed by alternative techniques [7]. To realize this targeted MS/MS experiment, the sample was first analyzed in MS-only mode using an LC-FTICR system, and the ARs of all detected peptide pairs were calculated. The m/z values and LC elution times for "interesting pairs", i.e., pairs showing differential abundance between the two isotopically labeled versions of the peptide, were consolidated into an "attention list." Next...

show abstract

Open trapped ion cell geometries for Fourier transform ion cyclotron resonance mass spectrometry

Cited by 124 publications

References 26 publications

Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry

Characterization of the P13 membrane protein of Borrelia burgdorferi by mass spectrometry

Vacuum compatible sample positioning device for matrix assisted laser desorption/ionization Fourier transform ion cyclotron resonance mass spectrometry imaging

Targeted tandem mass spectrometry for high-throughput comparative proteomics employing NanoLC-FTICR MS with external ion dissociation

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