A Transferable, Sample-Independent Calibration Procedure for Trapped Ion Mobility Spectrometry (TIMS)

Chai, Mengqi; Young, Meggie N.; Liu, Fanny C.; Bleiholder, Christian

doi:10.1021/acs.analchem.8b01326

Cited by 63 publications

(85 citation statements)

References 47 publications

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“…Cross sections determined for ubiquitin closely match the drift tube values. Overall, this calibration scheme reproduces drift tube ion mobilities within 1% (Chai et al, ).…”

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 66%

“…Commercial instruments use the Agilent tuning mixture as calibrants. However, the values currently embedded in the calibration files (Chai et al, ) differ by 0.75% on average from those reported from DTIMS (Stow et al, ) and used to calibrate the single‐field measurement in Agilent instruments. Thus, a significant bias between two methods (DTIMS vs. TIMS) is directly attributable to the choice of primary values for the calibrant ions, rather than the measurement principle or instrument design.…”

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

“…This is a consequence of the empirical nature of the calibration function. Hence, the calibrated coefficients are only valid for the exact TIMS settings (scan rate, range and pressure) used for their determination (Chai et al, ).…”

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

“…A transferable and sample‐independent calibration procedure was recently reported for TIMS based on a Taylor expansion of instrument properties (TEIP) (Chai et al, ). This is based on a calibration function derived from a solution to the Boltzmann transport equation, instead of from empirical correlations.…”

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

“…Finally, a Taylor‐expansion is performed for the instrument‐dependent quantities, and the resulting coefficients form the basis for the coefficients. These calibration coefficients were found, to a good approximation, constant over time and independent of instrument settings or sample properties (Chai et al, ).…”

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

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Recommendations for reporting ion mobility Mass Spectrometry measurements

Gabelica

Shvartsburg

Afonso

et al. 2019

Mass Spectrometry Reviews

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361

477

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Here we present a guide to ion mobility mass spectrometry experiments, which covers both linear and nonlinear methods: what is measured, how the measurements are done, and how to report the results, including the uncertainties of mobility and collision cross section values. The guide aims to clarify some possibly confusing concepts, and the reporting recommendations should help researchers, authors and reviewers to contribute comprehensive reports, so that the ion mobility data can be reused more confidently. Starting from the concept of the definition of the measurand, we emphasize that (i) mobility values ( K 0 ) depend intrinsically on ion structure, the nature of the bath gas, temperature, and E / N ; (ii) ion mobility does not measure molecular surfaces directly, but collision cross section (CCS) values are derived from mobility values using a physical model; (iii) methods relying on calibration are empirical (and thus may provide method‐dependent results) only if the gas nature, temperature or E / N cannot match those of the primary method. Our analysis highlights the urgency of a community effort toward establishing primary standards and reference materials for ion mobility, and provides recommendations to do so. © 2019 The Authors. Mass Spectrometry Reviews Published by Wiley Periodicals, Inc.

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“…Cross sections determined for ubiquitin closely match the drift tube values. Overall, this calibration scheme reproduces drift tube ion mobilities within 1% (Chai et al, ).…”

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 66%

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

Section: Reporting Ion Mobility Measurementsmentioning

confidence: 99%

See 3 more Smart Citations

Recommendations for reporting ion mobility Mass Spectrometry measurements

Gabelica

Shvartsburg

Afonso

et al. 2019

Mass Spectrometry Reviews

Self Cite

361

477

View full text Add to dashboard Cite

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Native mass spectrometry—A valuable tool in structural biology

Barth

Schmidt

2020

J Mass Spectrom

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Proteins and the complexes they form with their ligands are the players of cellular action. Their function is directly linked with their structure making the structural analysis of protein-ligand complexes essential. Classical techniques of structural biology include X-ray crystallography, nuclear magnetic resonance spectroscopy and recently distinguished cryo-electron microscopy. However, protein-ligand complexes are often dynamic and heterogeneous and consequently challenging for these techniques. Alternative approaches are therefore needed and gained importance during the last decades. One alternative is native mass spectrometry, which is the analysis of intact protein complexes in the gas phase. To achieve this, sample preparation and instrument conditions have to be optimised. Native mass spectrometry then reveals stoichiometry, protein interactions and topology of protein assemblies. Advanced techniques such as ion mobility and high-resolution mass spectrometry further add to the range of applications and deliver information on shape and microheterogeneity of the complexes. In this tutorial, we explain the basics of native mass spectrometry including sample requirements, instrument modifications and interpretation of native mass spectra. We further discuss the developments of native mass spectrometry and provide example spectra and applications.

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Collision cross section measurement and prediction methods in omics

Kartowikromo,

Olajide,

Hamid

2023

J Mass Spectrom

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Omics studies such as metabolomics, lipidomics, and proteomics have become important for understanding the mechanisms in living organisms. However, the compounds detected are structurally different and contain isomers, with each structure or isomer leading to a different result in terms of the role they play in the cell or tissue in the organism. Therefore, it is important to detect, characterize, and elucidate the structures of these compounds. Liquid chromatography and mass spectrometry have been utilized for decades in the structure elucidation of key compounds. While prediction models of parameters (such as retention time and fragmentation pattern) have also been developed for these separation techniques, they have some limitations. Moreover, ion mobility has become one of the most promising techniques to give a fingerprint to these compounds by determining their collision cross section (CCS) values, which reflect their shape and size. Obtaining accurate CCS enables its use as a filter for potential analyte structures. These CCS values can be measured experimentally using calibrant‐independent and calibrant‐dependent approaches. Identification of compounds based on experimental CCS values in untargeted analysis typically requires CCS references from standards, which are currently limited and, if available, would require a large amount of time for experimental measurements. Therefore, researchers use theoretical tools to predict CCS values for untargeted and targeted analysis. In this review, an overview of the different methods for the experimental and theoretical estimation of CCS values is given where theoretical prediction tools include computational and machine modeling type approaches. Moreover, the limitations of the current experimental and theoretical approaches and their potential mitigation methods were discussed.

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A Transferable, Sample-Independent Calibration Procedure for Trapped Ion Mobility Spectrometry (TIMS)

Cited by 63 publications

References 47 publications

Recommendations for reporting ion mobility Mass Spectrometry measurements

Recommendations for reporting ion mobility Mass Spectrometry measurements

Native mass spectrometry—A valuable tool in structural biology

Collision cross section measurement and prediction methods in omics

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