High Sensitivity Collisionally-activated Decomposition Tandem Mass Spectrometry on a Novel Quadrupole/Orthogonal-acceleration Time-of-flight Mass Spectrometer

Morris, Howard R.; Paxton, Thanai; Dell, Anne; Langhorne, Jean; Berg, Matthias; Bordoli, Robert S.; Hoyes, John; Bateman, Robert

doi:10.1002/(sici)1097-0231(19960610)10:8<889::aid-rcm615>3.0.co;2-f

Cited by 404 publications

(57 citation statements)

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“…One key pioneering example was the analysis of the enzyme 4-oxalocrotonate tautomerase [39], which upon ESI-MS analysis confirmed the oligomeric status of the enzyme, one of the leading examples at the time that native protein structures could be preserved into the gas phase for analysis. With the knowledge that noncovalent protein complexes could be analyzed, Sciex and Micromass Ltd. modified their quadrupole (Q)-ToF mass spectrometers [40, 41], which together with elegant work on the optimization and transmission of high m / z ions [42, 43], enabled tandem MS experiments to be performed on large protein complexes, providing information not only on protein complex stoichiometry but also on protein complex topology [41, 44, 45]. The Q-ToF technology rapidly became the platform most successful for native MS analysis, whereby the samples amendable for mass analysis reached sizes/molecular weights of over several million Daltons [46].…”

Section: Key Milestones In Native Msmentioning

confidence: 99%

Native Mass Spectrometry: What is in the Name?

Leney

Heck

2016

J. Am. Soc. Mass Spectrom.

496

480

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Electrospray ionization mass spectrometry (ESI-MS) is nowadays one of the cornerstones of biomolecular mass spectrometry and proteomics. Advances in sample preparation and mass analyzers have enabled researchers to extract much more information from biological samples than just the molecular weight. In particular, relevant for structural biology, noncovalent protein–protein and protein–ligand complexes can now also be analyzed by MS. For these types of analyses, assemblies need to be retained in their native quaternary state in the gas phase. This initial small niche of biomolecular mass spectrometry, nowadays often referred to as “native MS,” has come to maturation over the last two decades, with dozens of laboratories using it to study mostly protein assemblies, but also DNA and RNA-protein assemblies, with the goal to define structure–function relationships. In this perspective, we describe the origins of and (re)define the term native MS, portraying in detail what we meant by “native MS,” when the term was coined and also describing what it does (according to us) not entail. Additionally, we describe a few examples highlighting what native MS is, showing its successes to date while illustrating the wide scope this technology has in solving complex biological questions. Graphical Abstractᅟ

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Section: Key Milestones In Native Msmentioning

confidence: 99%

Native Mass Spectrometry: What is in the Name?

Leney

Heck

2016

J. Am. Soc. Mass Spectrom.

496

480

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“…While other mass analysers have been used to examine intact protein complexes [48], the ‘hybrid’ Q-ToF has been the favoured instrument geometry for about a decade [32], capitalizing on the m/z -range benefits of ToF with the selection abilities of a quadrupole (Q) [49]. The decreased resolution of this first analyser does not impact on the final spectrum, as this is determined by the subsequent ToF stage.…”

Section: The Development Of Ms For Structural Biologymentioning

confidence: 99%

Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry

Hilton

Benesch

2012

J. R. Soc. Interface.

130

122

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Mass spectrometry (MS) is a recognized approach for characterizing proteins and the complexes they assemble into. This application of a long-established physico-chemical tool to the frontiers of structural biology has stemmed from experiments performed in the early 1990s. While initial studies focused on the elucidation of stoichiometry by means of simple mass determination, developments in MS technology and methodology now allow researchers to address questions of shape, inter-subunit connectivity and protein dynamics. Here, we chart the remarkable rise of MS and its application to biomolecular complexes over the last two decades.

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“…Hybrid orthogonal-acceleration quadrupole time-of-flight (oa-QTOF) mass spectrometers have been commercially available for over ten years. 1 The instrument combines a series of multipoles (allowing ion selection and collision-induced dissociation (CID)) prior to the orthogonal-acceleration timeof-flight (oa-TOF) mass spectrometer. An extensive review of the principles of the original oa-QTOF technology was published in 2001.…”

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confidence: 99%

Performance optimisation of a new‐generation orthogonal‐acceleration quadrupole‐time‐of‐flight mass spectrometer

Bristow

Constantine

Harrison

et al. 2008

Rapid Comm Mass Spectrometry

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Orthogonal-acceleration quadrupole time-of-flight (oa-QTOF) mass spectrometers, employed for accurate mass measurement, have been commercially available for well over a decade. A limitation of the early instruments of this type was the narrow ion abundance range over which accurate mass measurements could be made with a high degree of certainty. Recently, a new generation of oa-QTOF mass spectrometers has been developed and these allow accurate mass measurements to be recorded over a much greater range of ion abundances. This development has resulted from new ion detection technology and improved electronic stability or by accurate control of the number of ions reaching the detector. In this report we describe the results from experiments performed to evaluate the mass measurement performance of the Bruker micrOTOF-Q, a member of the new-generation oa-QTOFs. The relationship between mass accuracy and ion abundance has been extensively evaluated and mass measurement accuracy remained stable (+/-1.5 m m/z units) over approximately 3-4 orders of magnitude of ion abundance. The second feature of the Bruker micrOTOF-Q that was evaluated was the SigmaFit function of the software. This isotope pattern-matching algorithm provides an exact numerical comparison of the theoretical and measured isotope patterns as an additional identification tool to accurate mass measurement. The smaller the value, the closer the match between theoretical and measured isotope patterns. This information is then employed to reduce the number of potential elemental formulae produced from the mass measurements. A relationship between the SigmaFit value and ion abundance has been established. The results from the study for both mass accuracy and SigmaFit were employed to define the performance criteria for the micrOTOF-Q. This provided increased confidence in the selection of elemental formulae resulting from accurate mass measurements.

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High Sensitivity Collisionally-activated Decomposition Tandem Mass Spectrometry on a Novel Quadrupole/Orthogonal-acceleration Time-of-flight Mass Spectrometer

Cited by 404 publications

References 0 publications

Native Mass Spectrometry: What is in the Name?

Native Mass Spectrometry: What is in the Name?

Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry

Performance optimisation of a new‐generation orthogonal‐acceleration quadrupole‐time‐of‐flight mass spectrometer

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