Maxis 4 g q tof ms

Manufactured by Bruker

Sourced in Germany

The Maxis 4 G Q-TOF MS is a high-resolution quadrupole time-of-flight mass spectrometer designed for accurate mass measurements and comprehensive analysis of complex samples. It provides precise mass determination with high sensitivity and resolution.

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Lab products found in correlation

Graphitized carbon cartridges, by Thermo Fisher Scientific (1 mentions) Msd 5975, by Agilent Technologies (1 mentions) Gc 7820a, by Agilent Technologies (1 mentions) J w hp 5ms gc column, by Agilent Technologies (1 mentions) Autoflex maldi tof, by Bruker (1 mentions) Dataanalysis 4, by Bruker (1 mentions) Ultimate 3000, by Bruker (1 mentions) Dionex ultimate 3000 uplc system, by Thermo Fisher Scientific (1 mentions) Maxis 4g hr tof mass spectrometer, by Bruker (1 mentions)

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Maxis Q-TOF (20 citations)

4 protocols using maxis 4 g q tof ms

N-Glycan Fractionation and Analysis

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Reducing N‐glycans were fractionated on a TSK‐amide 80 column (Tosoh Bioscence GmbH, www.tosohbioscience.com) as described (Grass et al., 2011), except that underivatized glycans were used. Therefore, fractions were analyzed for glycans by MALDI‐TOF MS.
For analytical purposes, the glycans were reduced with NaBH₄, desalted by passage over graphitized carbon cartridges (ThermoFisher Scientific, www.thermofisher.com) and subjected to LC‐ESI‐MS with a PGC column (0.32 μm × 150 mm) operated by an ultimate rapid separation LC (RSLC) system (ThermoFisher Scientific) connected to a Maxis 4 G Q‐TOF MS (Bruker) or an amaZone ion trap (Bruker), operating in data‐dependent acquisition mode (Pabst et al., 2012). The PGC column was eluted with 65 mm ammonium formate at pH 3.0 and a gradient from 8 to 60% acetonitrile in 50 min at a flow rate of 6 µl min⁻¹ at ambient temperature.

Mócsai R., Figl R., Sützl L., Fluch S, & Altmann F. (2020). A first view on the unsuspected intragenus diversity of N‐glycans in Chlorella microalgae. The Plant Journal, 103(1), 184-196.

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Structural Analysis of Glycans by MALDI-TOF and LC-ESI-MS

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MALDI-TOF MS of glycan pools was performed with dihydroxybenzoic acid as the matrix on a Bruker Autoflex MALDI-TOF instrument in the positive ion reflectron mode. Usually, unreduced samples were analyzed, but in some cases reduction with 1% sodium borohydride was done to readily discriminate glycan from non-glycan peaks.
Reduced glycans were analyzed by LC-ESI-MS with a porous graphitic carbon (PGC) column (0.32 µm x 150 mm) operated by an Ultimate RSLC (Thermo Scientific, Vienna) connected to a Maxis 4 G Q-TOF MS (Bruker, Bremen, Germany)^{25 (link)}. N-glycans from white kidney beans were used as reference^{25 (link)}. MS/MS was performed in positive mode.
The monosaccharide constituents were analyzed after hydrolysis of glycan pools of fractions with 4 M trifluoroacetic acid at 100° for 4 h. Sugars were reduced with NaBD₄, peracetylated and analyzed on an Agilent J&W HP-5ms GC Column (30 m x 0.25 mm, 0.25 µm) installed in a GC-MS system (GC 7820 A & MSD 5975, Agilent, Waldbronn, Germany). Partially methylated alditol acetates were available from a previous study^{29 (link)} and their relative retention times were additionally confirmed by literature data³⁰.

Mócsai R., Figl R., Troschl C., Strasser R., Svehla E., Windwarder M., Thader A, & Altmann F. (2019). N-glycans of the microalga Chlorella vulgaris are of the oligomannosidic type but highly methylated. Scientific Reports, 9, 331.

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Mass Spectrometry Analysis of Purified Enzyme

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The purified enzyme was analyzed by liquid chromatography mass spectrometry (LC–ESI–MS) using a Dionex Ultimate 3000 capillary LC and a Bruker maXis 4G Q-TOF MS. Separation of the different truncated versions was performed using a reverse phase Supelco Discovery Bio Wide Pore C5 column (50 * 0.32 mm, 3 μm packing) with elution achieved by using a gradient of 55 min from 5% acetonitrile (solvent A: 0.1% formic acid) to 80% acetonitrile.
Data generated by mass spectrometry was processed using Data Analysis 4 (Bruker Daltonics) and MASCOT [28] (link). Deconvolution was performed using MaxEnt software (Micromass, Manchester, UK).

Plattner S., Gruber C., Altmann F, & Bohlmann H. (2014). Self-processing of a barley subtilase expressed in E. coli. Protein Expression and Purification, 101, 76-83.

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Recombinant Protein Analysis by LC-QTOF

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Recombinant proteins were analyzed on a Dionex Ultimate 3000 UPLC system (Thermo Scientific™)
coupled with an maXis4G Q-TOF MS (Bruker) using an ESI in positive mode. The samples were run on an Aeris Widepore XB-C8, 150 x 2.1 mm, 3.6 μm dp column (Phenomenex, USA). LC conditions:
A: H2O + 0.1% FA; B: ACN + 0.1% FA at a flow rate of 300 μL/min and 45 °C. 0 min: 98% A / 2% B, 0.5 min: 98% A / 2% B, 10.5 min: 25% A / 75% B, 13.5 min: 25% A / 75% B, 14 min: 98% A / 2% B.
The LC flow was split to 75 μL/min before entering the maXis4G hr-ToF mass spectrometer (Bruker Daltonics, Bremen, Germany) using the standard Bruker ESI source. In the source region, the temperature was set to 180 °C, the capillary voltage was 4000 V, the dry-gas flow was 6.0 L/min and the nebulizer was set to 1.1 bar. Mass spectra were acquired in positive ionization mode ranging from 150-2500 m/z at 2.5 Hz scan rate. Protein masses were deconvoluted by using the Maximum Entropy algorithm (Copyright 1991-2004 Spectrum Square Associates, Inc.).

Hug J.J., Dastbaz J., Adam S., Revermann O., Koehnke J., Krug D, & Müller R. (2020). Biosynthesis of Cittilins, Unusual Ribosomally Synthesized and Post-translationally Modified Peptides from Myxococcus xanthus. ACS chemical biology, 15(8).

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