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Q exactive hf quadrupole orbitrap

Manufactured by Thermo Fisher Scientific
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The Q Exactive HF quadrupole-orbitrap is a high-resolution, accurate-mass (HRAM) mass spectrometer. It combines a quadrupole mass filter with an Orbitrap mass analyzer, enabling high-resolution, accurate-mass measurement of ions.

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Lab products found in correlation

Byonic v2, by Protein Metrics (1 mentions) Ultimate 3000 system, by Thermo Fisher Scientific (1 mentions) Byonic, by Protein Metrics (1 mentions)

Close spelling variants of this product

Q Exactive HF Hybrid Quadrupole-Orbitrap MS Thermo Q Exactive HF Hybrid Quadrupole-Orbitrap Mass Spectrometer Q Exactive HF-X hybrid Quadrupole-Orbitrap Q Exactive HF Hybrid Quadrupole-Orbitrap Mass Spectrometer Q Exactive HF Hybrid Quadrupole-Orbitrap Q Exactive HF-X Quadrupole-Orbitrap mass spectrometer Q Exactive HF‐X Hybrid Quadrupole‐Orbitrap MS LC–ESI–MS-MS Q Exactive HF hybrid quadrupole-Orbitrap mass spectrometer Q Exactive HF-X Hybrid Quadrupole-Orbitrap Mass Spectrometer Q-Exactive HF quadrupole-Orbitrap mass spectrometer

2 protocols using q exactive hf quadrupole orbitrap

1

Proteomic Analysis of Rps. palustris

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Digested samples were redissolved in 0.1% TFA, 3% acetonitrile and analysed by nano-flow liquid chromatography (Ultimate 3000 system, Thermo Scientific) coupled on-line to a mass spectrometer (Amazon ion trap, Bruker or Q Exactive HF quadrupole-orbitrap, Thermo Scientific). For protein identification, Amazon MS data-files were first converted to Mascot Generic File (MGF) format using a script provided by Bruker. Amazon MGF and Q Exactive RAW data-files were uploaded into Byonic v. 2.9.38 (Protein Metrics) for searching against the Uniprot reference proteome database for Rps. palustris (ID: UP000001426, 4811 entries, 9 July 2016).
Jackson P.J., Hitchcock A., Swainsbury D.J., Qian P., Martin E.C., Farmer D.A., Dickman M.J., Canniffe D.P, & Hunter C.N. (2018). Identification of protein W, the elusive sixth subunit of the Rhodopseudomonas palustris reaction center-light harvesting 1 core complex. Biochimica et Biophysica Acta, 1859(2), 119-128.
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2

Comprehensive Proteomic Analysis of RC-LH1 Complex

Cited 2 times
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Pure RC-LH1 core complex (50 µg) was solubilised and digested with pepsin, and the resulting peptides were analysed by nano-flow liquid chromatography coupled to a Q Exactive HF quadrupole-Orbitrap (Thermo Scientific) mass spectrometer as described in our previous work [10 (link),38 (link)]. Protein identification was performed by database searching using Byonic (v2.9.38, Protein Metrics) operating with the default parameters except that methionine sulfoxide (+15.19949 Da) was specified as a common variable modification (with a maximum of two per peptide). Cleavage sites were specified as N- and C-terminal to F, Y, W and L (semi-specific). The database was the Rba. sphaeroides reference proteome (www.uniprot.org/proteomes/ UP000002703) downloaded on 28 April 2021 and edited by adding the putative protein-Z sequence derived by the re-annotation of the Rsp_2385 locus (see Supplementary Figure S2).
Qian P., Croll T.I., Hitchcock A., Jackson P.J., Salisbury J.H., Castro-Hartmann P., Sader K., Swainsbury D.J, & Hunter C.N. (2021). Cryo-EM structure of the dimeric Rhodobacter sphaeroides RC-LH1 core complex at 2.9 Å: the structural basis for dimerisation. Biochemical Journal, 478(21), 3923-3937.
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