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Lct premier instrument

Manufactured by Waters Corporation
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Sourced in United States

The LCT Premier instrument is a liquid chromatography-time of flight mass spectrometer (LC-TOF MS) designed for high-resolution, accurate-mass analysis. It provides precise mass measurements and high sensitivity for a wide range of applications in analytical chemistry and life sciences.

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Lab products found in correlation

1200 system, by Agilent Technologies (2 mentions) 6410 qqq mass spectrometer, by Agilent Technologies (2 mentions) Cary 50 spectrometer, by Agilent Technologies (2 mentions) Av 3 hd 500, by Bruker (1 mentions) Agilent 1100 series, by Agilent Technologies (1 mentions) Agilent 1100 series system, by Agilent Technologies (1 mentions)

3 protocols using lct premier instrument

1

Multimodal Characterization of Biomolecules

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Size-exclusion chromatography was conducted using a HiPrep 16/60 Sephadex S-200 column connected to an ÅKTA fast pro-tein liquid chromatography (FPLC) system in a Coy anaerobic chamber (Grass Lake, MI). UV-visible spectra were recorded on a Cary 50 spectrometer from Varian (now Agilent Technologies) using the WinUV software package to control the instrument. High performance liquid chromatography (HPLC) with detection by tandem mass spectrometry (LC-MS/MS) was conducted on an Agilent Technologies (Santa Clara, CA) 1200 system coupled to an Agilent Technologies 6410 QQQ mass spectrometer. The system was operated with the associated MassHunter software package, which was also used for data collection and analysis. High-resolution ESI mass spectra were acquired in on a Waters LCT Premier instrument at the Penn State Huck Institute of Life Sciences proteomics and mass spectrometry core facility. DNA sequencing was conducted at the Huck Institutes of the Life Sciences genomics core facility. NMR spectra were recorded on a Bruker AV-3-HD-500 instrument and calibrated using residual solvent peaks as an internal reference. Multiplicities are recorded as: s = singlet, d = doublet, t = triplet, dd = doublet of doublets, m = multiplet, q = quartet, dt = doublet of triplets.
LaMattina J.W., Wang B., Badding E.D., Gadsby L.K., Grove T.L, & Booker S.J. (2017). The Radical S-Adenosylmethionine Methylase NosN Catalyzes both C1 Transfer and Formation of the Ester Linkage of the Side-Ring System during the Biosynthesis of Nosiheptide. Journal of the American Chemical Society, 139(48), 17438-17445.
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2

Characterization of Organic Compounds

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NMR experiments were performed using a Varian NMR System 600-MHz instrument (Palo Alto, CA, USA) and JEOL NMR Systems 400-MHz and 500-MHz instruments (Tokyo, Japan). The chemical shifts are reported in ppm, and each coupling constant (J) is reported in Hz. Electron spray ionization (ESI) high-resolution mass spectra were acquired on a Bruker Daltonics MicrOTOF II instrument (Bremen, Germany) and a Waters LCT Premier instrument (Milford, MA, USA).
Koga T., Kawahara N., Aburada M., Ono A., Mae S., Yoshida A., Iwaoka Y., Ito H, & Tai A. (2023). Antiallergic Activity of 3-O-Dodecyl-l-ascorbic Acid. Molecules, 29(1), 69.
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3

Multi-instrument Analysis of Organic Compounds

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UV-visible spectra were recorded on a Cary 50 spectrometer from Varian (Agilent Technologies, Santa Clara, CA) using the WinUV software package to control the instrument. High-performance liquid chromatography (HPLC) with detection by tandem mass spectrometry (LC-MS/MS) was conducted on an Agilent Technologies 1200 system coupled to an Agilent Technologies 6410 QQQ mass spectrometer. The system was operated with the associated MassHunter software package, which was also used for data collection and analysis. HPLC was also conducted on an Agilent 1100 Series system coupled to an Agilent 1100 Series variable wavelength detector and quaternary pump. NMR spectra of all compounds were collected on a Bruker AV-3-HD-500 instrument. High-resolution ESI mass spectra were collected on a Waters LCT Premier instrument.
Wang B., LaMattina J.W., Marshall S.L, & Booker S.J. (2019). Capturing Intermediates in the Reaction Catalyzed by NosN, a Class C Radical S-Adenosylmethionine Methylase Involved in the Biosynthesis of the Nosiheptide Side Ring System. Journal of the American Chemical Society, 141(14), 5788-5797.
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