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Qtof 6510

Manufactured by Agilent Technologies
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The QTOF 6510 is a high-resolution quadrupole time-of-flight mass spectrometer designed for accurate mass and structural analysis. It provides high-resolution mass spectrometry capabilities for applications such as small molecule analysis, peptide and protein characterization, and metabolite profiling.

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Lab products found in correlation

Masshunter software, by Agilent Technologies (7 mentions) Vivaspin, by Sartorius (6 mentions) Agilent 1200 series lc, by Agilent Technologies (3 mentions) Agilent mass hunter software, by Agilent Technologies (1 mentions)

9 protocols using qtof 6510

1

Characterization of Au25(Cys)18 Nanoclusters

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To characterise [Au25(Cys)18], the dried nanoclusters were mixed with DI water containg 0.01 µM cesium acetate, and then the solution was infused into an electrospray ionization-mass spectrometer (ESI-MS, Q-TOF 6510, Agilent Technology) at a flow rate of 20 µL min−1. The electrospray ionization (ESI) was operated in negative mode, and heated nitrogen (the drying gas) was supplied into the spectrometer at a flow rate of 5 L min−1. The negatively charged ions were analysed by mass spectrometer (MS).
Hwang G.B., Huang H., Wu G., Shin J., Kafizas A., Karu K., Toit H.D., Alotaibi A.M., Mohammad-Hadi L., Allan E., MacRobert A.J., Gavriilidis A, & Parkin I.P. (2020). Photobactericidal activity activated by thiolated gold nanoclusters at low flux levels of white light. Nature Communications, 11, 1207.
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2

Protein Cofactor Desalting and Mass Spectrometry

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Samples were prepared by a desalting of proteins into 100 mm ammonium acetate, pH 7.0. A 1200 series Agilent LC was used to inject 5 μl of sample into 5% acetonitrile (0.1% formic acid) and desalted inline to release the cofactor from the enzyme complex. This was eluted over 1 min by 95% acetonitrile. The resulting ions were analyzed by an Agilent QTOF 6510 run in positive mode and deconvoluted using Agilent Masshunter software.
Bailey S.S., Payne K.A., Fisher K., Marshall S.A., Cliff M.J., Spiess R., Parker D.A., Rigby S.E, & Leys D. (2017). The role of conserved residues in Fdc decarboxylase in prenylated flavin mononucleotide oxidative maturation, cofactor isomerization, and catalysis. The Journal of Biological Chemistry, 293(7), 2272-2287.
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3

Protein Mass Spectrometry Protocol

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Purified protein samples were buffer-exchanged
into 0.1% acetic acid using a 10K MWCO Vivaspin (Sartorius) and diluted
to a final concentration of 0.5 mg ml–1. MS was
performed using a 1200 series Agilent LC, 5 μL injection into
5% acetonitrile (with 0.1% formic acid), and desalted inline for 1
min. Protein was eluted over 1 min using 95% acetonitrile with 5%
water. The resulting multiply charged spectrum was analyzed using
an Agilent QTOF 6510 and deconvoluted using Agilent MassHunter Software.
All data are presented in Figure S1.
Ortmayer M., Fisher K., Basran J., Wolde-Michael E.M., Heyes D.J., Levy C., Lovelock S.L., Anderson J.L., Raven E.L., Hay S., Rigby S.E, & Green A.P. (2020). Rewiring the “Push-Pull” Catalytic Machinery of a Heme Enzyme Using an Expanded Genetic Code. ACS Catalysis, 10(4), 2735-2746.
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4

Mass Spectrometry Analysis of Proteins

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Purified protein samples were desalted into 0.1% acetic acid using a 10 k MWCO Vivaspin (Sartorius) and diluted to a final concentration of 0.5 mg mL−1. Mass spectrometry was performed using a 1200 series Agilent LC, with a 5 µL injection into 5% acetonitrile (with 0.1% formic acid) and desalted inline for 1 min. Protein was eluted over 1 min using 95% acetonitrile with 5% water. The resulting multiply charged spectrum was analysed using an Agilent QTOF 6510 and deconvoluted using Agilent MassHunter Software.
Hutton A.E., Foster J., Crawshaw R., Hardy F.J., Johannissen L.O., Lister T.M., Gérard E.F., Birch-Price Z., Obexer R., Hay S, & Green A.P. (2024). A non-canonical nucleophile unlocks a new mechanistic pathway in a designed enzyme. Nature Communications, 15, 1956.
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5

Protein Sample Preparation for Mass Spectrometry

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Purified protein samples were buffer exchanged into 0.1% acetic acid using a 10k mwco Vivaspin® (Sartorius) and diluted to a final concentration of 0.5 mg/mL. MS analysis was performed using a 1200 series Agilent LC, 5 μL injection into 5% acetonitrile (with 0.1% formic acid) and desalted inline for 1 min. Protein was eluted over 1 min using 95% acetonitrile with 5% water. The resulting multiply charged spectrum was analyzed using an Agilent QTOF 6510 and deconvoluted using Agilent MassHunter Software.
Taylor C.J., Hardy F.J., Burke A.J., Bednar R.M., Mehl R.A., Green A.P, & Lovelock S.L. (2023). Engineering mutually orthogonal PylRS/tRNA pairs for dual encoding of functional histidine analogues. Protein Science : A Publication of the Protein Society, 32(5), e4640.
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6

Protein Identification by LC-QTOF MS

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A 1200 series Agilent LC was used to inject 5 µL of sample into 5% acetonitrile (0.1% formic acid) and desalted inline. This was eluted over 1 min by 95% acetonitrile. The resulting multiply charged spectrum was analysed by an Agilent QTOF 6510, and deconvoluted using Agilent Masshunter Software.
Horga L.G., Halliwell S., Castiñeiras T.S., Wyre C., Matos C.F., Yovcheva D.S., Kent R., Morra R., Williams S.G., Smith D.C, & Dixon N. (2018). Tuning recombinant protein expression to match secretion capacity. Microbial Cell Factories, 17, 199.
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7

Mass Spectrometry of Protein Samples

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Purified protein samples were buffer exchanged into 0.1% acetic acid using a 10k MWCO Vivaspin (Sartorius) and diluted to a final concentration of 0.5 mg mL−1. Mass spectrometry was performed using a 1200 series Agilent LC, with a 5 μL injection into 5% acetonitrile (with 0.1% formic acid) and desalted inline for 1 min. Protein was eluted over 1 min using 95% acetonitrile with 5% water. The resulting multiply charged spectrum was analysed using an Agilent QTOF 6510 and deconvoluted using Agilent MassHunter Software.
Crawshaw R., Crossley A.E., Johannissen L., Burke A.J., Hay S., Levy C., Baker D., Lovelock S.L, & Green A.P. (2021). Engineering an Efficient and Enantioselective Enzyme for the Morita-Baylis-Hillman Reaction. Nature chemistry, 14(3), 313-320.
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8

Mass Spectrometry of Protein Samples

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Purified protein samples were buffer exchanged into 0.1% acetic acid using a 10k MWCO Vivaspin (Sartorius) and diluted to a final concentration of 0.5 mg mL−1. Mass spectrometry was performed using a 1200 series Agilent LC, with a 5 μL injection into 5% acetonitrile (with 0.1% formic acid) and desalted inline for 1 min. Protein was eluted over 1 min using 95% acetonitrile with 5% water. The resulting multiply charged spectrum was analysed using an Agilent QTOF 6510 and deconvoluted using Agilent MassHunter Software.
Crawshaw R., Crossley A.E., Johannissen L., Burke A.J., Hay S., Levy C., Baker D., Lovelock S.L, & Green A.P. (2021). Engineering an Efficient and Enantioselective Enzyme for the Morita-Baylis-Hillman Reaction. Nature chemistry, 14(3), 313-320.
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9

Protein Desalting and Mass Spectrometry

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Purified protein samples were desalted on 10k MWCO Vivaspin centrifugal concentrators (Sartorius) using 0.1% acetic acid and diluted to a final concentration of 0.4 mg mL -1 . Mass spectrometry was performed on a 1200 series Agilent LC in conjunction with a Agilent QTOF 6510. A 5 µL sample injection was performed followed by a 1 min 5% acetonitrile (with 0.1% formic acid) isocratic wash. Protein was eluted over 1 min using 95% acetonitrile with 5% water. The resulting multiply charged spectrum was deconvoluted using Agilent MassHunter Software. Protein mass spectrometry results are displayed in Supplementary Information, Table S7.
Trimble J.S., Crawshaw R., Hardy F.J., Levy C.W., Brown M.J.B., Fuerst D.E., Heyes D.J., Obexer R, & Green A.P. (2022). A designed photoenzyme for enantioselective [2+2] cycloadditions. Nature, 611(7937).
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