Intact protein mass measurements of purified SUMO-sfGFP variants were performed by electrospray LC-MS on a Waters H-class instrument with a Waters Acquity UPLC protein BEH C4 column (300 Å, 1.7 μm, 2.1 mm × 50 mm). The following gradient used a flow rate of 0.3 mL/min: A: 0.01% formic acid in H2O; B: 0.01% formic acid in MeCN. 5–95% B 0–6 min. Mass analysis was conducted with a Waters Xevo G2-XS QTof analyzer. Proteins were ionized in positive ion mode applying a cone voltage of 40 kV. Raw data were analyzed employing the maximum entropy deconvolution algorithm. The data were exported and plotted with QtiPlot (version 0.9.9.7).
H class instrument
Manufactured by Waters Corporation
Sourced in United States
The H-class instrument is a high-performance liquid chromatography (HPLC) system designed for analytical and preparative applications. It provides reliable and accurate separation, identification, and quantification of a wide range of chemical compounds. The H-class instrument is capable of delivering precise solvent flow and gradient programming, enabling efficient and reproducible analysis across a variety of sample types.
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Lab products found in correlation
6 protocols using h class instrument
1
Intact Protein Mass Measurements of SUMO-sfGFP
2
HPLC Analysis of Compounds
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A Waters H‐Class instrument (Waters) was used for HPLC analysis. Chromatographic separation was performed on a Hypersil GOLD column (1.9 μm, 100 mm × 2.1 mm) using 0.1% formic acid solution and acetonitrile as the mobile phase.
3
Analyzing ncAA Incorporation into OCP
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To identify ncAA incorporation into OCP by MmPylRS, intact protein masses were analyzed by an electrospray ionization mass spectrometry (ESI-MS) source (Waters H-class instrument). The proteins were eluted through an Acquity UPLC protein BEH C4 column (300 Å, 1.7 μm, 2.1 mm × 50 mm) with a flow rate of 0.3 mL/min. The resulting ions were analyzed by a Waters XEVO G2-XS QTof analyzer (Waters Corp., Milford, MA, United States). Spectra deconvolution was performed using MaxEnt 1 employing the maximum entropy deconvolution algorithm. Observed protein masses were compared to theoretical values determined by the Expasy ProtParam tool (Gasteiger et al., 2005 (link)).
4
Chemical Synthesis and Characterization of CBG/SBG-Linked Dyes
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Chemical synthesis (ESI Schemes S1 and S2† ) and characterization of compounds is outlined in the ESI.† Purity of all CBG/SBG-linked dyes was determined to be of >95% by UPLC-UV/Vis traces at 254 nm and dye specific λmax that were recorded on a Waters H-class instrument equipped with a quaternary solvent manager, a Waters autosampler, a Waters TUV detector and a Waters Acquity QDa detector with an Acquity UPLC BEH C18 1.7 μm, 2.1 × 50 mm RP column (Waters Corp., USA).
5
Quantitative SUMO-sfGFP Characterization
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Intact protein mass measurements of purified SUMO-sfGFP variants were performed by electrospray LC-MS on a Waters H-class instrument with a Waters Acquity UPLC protein BEH C4 column (300 Å, 1.7 μm, 2.1 × 50 mm, gradient at a flow rate of 0.3 ml/min: A: 0.01% formic acid in H2O; B: 0.01% formic acid in MeCN. 5–95% B 0–6 min). Mass analysis was conducted with a Waters Xevo G2-XS QTof analyzer (positive mode, cone voltage = 40 kV). Raw data were analyzed employing the maximum entropy deconvolution algorithm and plotted with Origin.
6
Chemical Synthesis and Characterization
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Chemical synthesis (ESI Schemes 1 and 2† ) and characterization of compounds is outlined in the ESI.† Purity of all dyes was determined to be of >95% by UPLC-UV/Vis traces at 254 nm and dye specific λmax that were recorded on a Waters H-class instrument equipped with a quaternary solvent manager, a Waters autosampler, a Waters TUV detector and a Waters Acquity QDa detector with an Acquity UPLC BEH C18 1.7 μm, 2.1 × 50 mm RP column (Waters Corp., USA).
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