Driftscope 2

Manufactured by Waters Corporation

Sourced in United Kingdom, United States

The DriftScope 2.7 is a laboratory instrument designed for the analysis and measurement of ion drift velocities. It provides precise data on the movement of charged particles within an electric field, enabling researchers to study ion mobility and transport phenomena.

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Driftscope (14 citations) Driftscope version 2.8 (10 citations)

20 protocols using driftscope 2

Ion Mobility Spectrometry Protocol

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The travelling wave IMS was done in both positive and negative mode, using
the same instrument, Synapt G2 Q-TOF-MS according to the method by Masike et
al.^{33 (link)} A ion mobility (IMS) wave height of 30.2 V and a
wave velocity of 387 m/s was used. The collision cross-section (CCS) values
and ion mobility constant (K) were calculated using polyalanine
calibrations. Data processing was done using Driftscope 2.9 software (Waters
Corporation, Milford, MA, USA).

Mafata M., Stander M., Masike K, & Buica A. (2023). Exploratory data fusion of untargeted multimodal LC-HRMS with annotation by LCMS-TOF-ion mobility: White wine case study. European Journal of Mass Spectrometry (Chichester, England), 29(2), 111-122.

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Ion Mobility and SID Subcomplexes Analysis

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Ion mobility was used to separate product ions and selection rules for each SID product were made using Waters Corporation Driftscope 2.9 software. The intensity of subcomplexes were extracted from SID spectra with TWIMExtract v1.3 (48 (link)). CE were calculated as

E (e V) = z V_{SID}

, where

z

is the charge state of the precursor ions and

V_{SID}

is the SID voltage. ERMS were corrected by

m_{Hfq Δ CTD} / m_{Hfq}

and

m_{Protein} / m_{Protein • RNA}

(see also SI Appendix, Eqs. S1–S3). Additional information provided in SI Appendix.

Sarni S.H., Roca J., Du C., Jia M., Li H., Damjanovic A., Małecka E.M., Wysocki V.H, & Woodson S.A. (2022). Intrinsically disordered interaction network in an RNA chaperone revealed by native mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America, 119(47), e2208780119.

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Oligosaccharide Quantification by IM-MS

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IM-MS data analysis was performed using MassLynx 4.1 and DriftScope 2.9 (Waters Corp., Milford, MA, USA). The [M + H]⁺, [M + Na]⁺, and [M + K]⁺ ions of PMP-derivatized oligosaccharides were extracted from the total ion chromatograms. The chromatographic peaks were integrated to sum the peak areas of PMP-derivatized oligosaccharides. Then, the resulting data set, containing information of oligosaccharides, peak area, and sample code, was generated as an excel file and imported into SIMCA software 14.1 (Umetrics, Umea, Sweden) to conduct the MDVA. Statistical significance was determined by Student’s t-test using SPSS 21 (IBM Corporation, Chicago, USA).

Shao S., Xu W., Xie Z., Li M., Zhao J., Yang X., Yu P, & Yang H. (2022). Distinctive carbohydrate profiles of black ginseng revealed by IM-MS combined with PMP labeling and multivariate data analysis. Current Research in Food Science, 5, 2243-2250.

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cIM-MS Glycan Analysis Protocol

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The cIM-MS instrument was controlled using MassLynx 4.2 software. The data were processed using MassLynx 4.2, DriftScope 2.9, and MS^EViewer (all from Waters, Wilmslow, U.K.). Arrival time distributions (ATDs) were smoothed in MassLynx 4.2 using the Savitzky–Golay algorithm (two iterations over three bins). Data interpretation was assisted by GlycoWorkbench^{35 (link)} and GAG-finder.^{36 (link)} Fragments were annotated according to the Domon and Costello³⁷ nomenclature.

Cavallero G.J, & Zaia J. (2022). Resolving Heparan Sulfate Oligosaccharide Positional Isomers Using Hydrophilic Interaction Liquid Chromatography-Cyclic Ion Mobility Mass Spectrometry. Analytical chemistry, 94(5), 2366-2374.

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HDMS-based Lipid Profiling Protocol

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Sections were coated NEDC as described above however, samples were analysed using a HDMS SYNAPT G2 HDMS system (Waters Corporation, UK) and Driftscope 2.1 software (Waters Corporation). MS/MS spectra were acquired by manually moving the laser position and adjusting the collision energy between 25-45 eV with acquisition times of 20 seconds per spectrum. MS/MS peak lists from each spectrum were uploaded onto LIPID MAPS (http://www.lipidmaps.org) for database search. Prior to analysis the instrument was calibrated using red phosphorous cluster ions.

Lewis E.E.L., Barrett M.R.T., Freeman-Parry L., Bojar R.A, & Clench M.R. (2018). Examination of the skin barrier repair/wound healing process using a living skin equivalent model and matrix-assisted laser desorption-ionization-mass spectrometry imaging. International journal of cosmetic science, 40(2).

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Mass Spectrometry Imaging of Lipids

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Mass spectrometry imaging was performed using a HDMS SYNAPT TM G2 system and Driftscope 2.1 software (Waters, UK). Mass spectrometry (MS) and tandem mass spectrometry (MS/MS) data were acquired in positive ion sensitivity mode at a mass resolution of 10 000 full width at half maximum (FWHM) with ion mobility separation enabled and over the mass range m/z 100 to 1200. Image acquisition was performed using raster imaging mode at 100 μm spatial resolution, Biomap 3.7.5.5 software (http://www.maldi-msi.org/) was used for image generation. The MS/MS spectra were acquired manually moving the laser position and adjusting the collision energy to achieve good signal to noise for product ions across the full m/z range of the spectrum. Collision energies were adjusted from 25 to 40 eV during acquisition and acquisition times were generally of the order of 5-10 s per spectrum. Lipids were identified by the comparison of the exact molecular masses and fragmentation pathways of the protonated molecule ions, recorded during the MS/ MS experiments, with LIPIDMAPS database (www. lipidmaps.org) Positive identification of molecular ions was assumed if a unique match with error below 3 ppm was found.

Wojakowska A., Cole L.M., Chekan M., Bednarczyk K., Maksymiak M., Oczko-Wojciechowska M., Jarząb B., Clench M.R., Polańska J., Pietrowska M, & Widlak P. (2018). Discrimination of papillary thyroid cancer from non-cancerous thyroid tissue based on lipid profiling by mass spectrometry imaging. Endokrynologia Polska, 69(1).

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MALDI-IMS Analysis of Plant Stem Tissues

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For the MALDI SYNAPT G1 and SYNAPT G2 analyses, both instruments comprised a traveling-wave ion mobility device, operated with the following settings: laser energy 300–250 Hz, trap collision energy 4 V, and transfer collision energy 30 V. The ion mobility cell was activated and operated with Nitrogen as drift gas, and the mass spectrometer was operated in positive ionization mode under HDMS mode, with a MS resolution of 10,000 in a drift range from 1 to 200 bins, and 0.25 ppm of lock mass tolerance, IMS wave velocity of 300 m/s and wave height 8 V. Mass spectrometry data was analyzed in MassLynx and DriftScope 2.8 software (Waters Corporation). IMS-MS was carried out on tissue printed stem sections (2 transverse and 2 longitudinal) and on extracts from dissected stem tissue from 4 individual plants (as shown in Figure 3A).

Pérez-López A.V., Simpson J., Clench M.R., Gomez-Vargas A.D, & Ordaz-Ortiz J.J. (2021). Localization and Composition of Fructans in Stem and Rhizome of Agave tequilana Weber var. azul. Frontiers in Plant Science, 11, 608850.

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Ion Mobility-MS/MS Lipid Profiling of PAK

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The lipids extracted from the membrane of PAK were reconstituted in chloroform/methanol ( MS/MS experiments were performed in both positive and negative ionization mode.
Precursor ions were selected in the quadrupole, at a resolution of 1 m/z unit, using retention time windows in the acquisition method. Several acquisitions were performed to obtain the MS/MS spectra for all co-eluting lipids. The collisional activation was performed in the trap cell using argon as target gas (6.10 -3 mbar) and a collision energy of 35 eV. MS/MS spectra were processed using MassLynx 4.1 (Waters).
For calibrants, raw data were first opened with DriftScope 2.8 (Waters) in order to only select the singly charged ions on the 2D map (drift times plotted against m/z). Ion mobility spectra were then exported and processed with MassLynx 4.1 (Waters). For PAK samples, raw data were processed with UNIFI 1.8.2.169 (Waters). PAK lipids were first manually identified in order to create a home-made library from retention time (t R ) and m/z, for each of the lipids described in this publication. This library was then used to automatically obtain the lipids t D .

Deschamps E., Schmitz-Afonso I., Schaumann A., Dé E., Loutelier-Bourhis C., Alexandre S, & Afonso C. (2019). Determination of the collision cross sections of cardiolipins and phospholipids from Pseudomonas aeruginosa by traveling wave ion mobility spectrometry-mass spectrometry using a novel correction strategy. Analytical and bioanalytical chemistry, 411(30).

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Traveling Wave Ion Mobility Mass Spectrometry

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Traveling
wave ion mobility
mass spectrometry (TWIMS-MS) experiments were performed with a Synapt
G2 HDMS quadrupole/time-of-flight mass spectrometer (Waters, Manchester,
UK) equipped with an ESI source operated in negative mode for the
present experiments. Samples were introduced at a 10 μL/min
flow rate (capillary voltage: 2.27 kV, sampling cone voltage: 50 V)
under a curtain gas (N₂) flow of 100 L/h at 35 ° C.
Accurate mass experiments were performed using reference ions from
the CH₃COONa external standard via a LockSpray
interface. All ESI-MS/MS spectra were recorded in the 50–1500 m/z range, with a trap bias DC voltage
of 45 V, a helium cell gas flow of 180 mL/min, and a trap collision
energy of 30 eV. For ESI-IM-MS/MS spectra, a transfer collision energy
of 30 eV was used. All data analyses were carried out using the MassLynx4.1
and DriftScope 2.1 programs provided by Waters. Drift times were correlated
to the CCSs using polyalanine oligomers to calibrate the mobility
data.^{48 (link)}

Corinti D., Chiavarino B., Spano M., Tintaru A., Fornarini S, & Crestoni M.E. (2021). Molecular Basis for the Remarkably Different Gas-Phase Behavior of Deprotonated Thyroid Hormones Triiodothyronine (T3) and Reverse Triiodothyronine (rT3): A Clue for Their Discrimination?. Analytical Chemistry, 93(44), 14869-14877.

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Ion Mobility Mass Spectrometry Protocol

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All experiments were performed using a Synapt HDMS quadrupole/time‐of‐flight (QTOF) mass spectrometer (Waters Corp., Milford, MA, USA) equipped with the traveling‐wave version of IM‐MS38 and ESI.22 (link), 23 (link) The IM region was located between the Q and TOF mass analyzers, within a triwave device consisting of three cells in the order trap cell, IM cell, and transfer cell. The trap and transfer cells were pressurized with Ar, and the IM cell with N₂. The following parameters were used: ESI capillary voltage, 3.2 kV; sample cone voltage, 35 V; extraction cone voltage, 3.2 V; desolvation gas flow rate, 500 L/h (N₂); trap collision energy (CE), 6 eV; transfer CE, 4 eV; trap gas flow rate, 1.5 mL/min (Ar); IM cell gas flow rate, 22.7 mL/min (N₂); sample flow rate, 5 μL/min; source temperature, 80°C; desolvation temperature, 150°C; IM traveling‐wave height, 7.5 V; and IM traveling‐wave velocity, 350 m/s. The sprayed solutions were prepared by dissolving the sample in MeCN at 0.05 mg/mL. Data analyses were conducted using the MassLynx 4.1 and DriftScope 2.1 programs provided by Waters.

Endres K.J., Barthelmes K., Winter A., Antolovich R., Schubert U.S, & Wesdemiotis C. (2020). Collision cross‐section analysis of self‐assembled metallomacrocycle isomers and isobars via ion mobility mass spectrometry. Rapid Communications in Mass Spectrometry, 34(Suppl 2), e8717.

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