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The ES388 is a laboratory centrifuge designed for general-purpose separations. It features a maximum speed of 6,000 rpm and an integrated timer. The centrifuge accommodates a variety of sample tubes and microplates.

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Lab products found in correlation

Q exactive uhmr, by Thermo Fisher Scientific (2 mentions) Zeba spin column, by Thermo Fisher Scientific (2 mentions)

2 protocols using es388

1

Direct Mass Technology for Single Ion Analysis

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Single ion measurement using Direct Mass Technology mode was performed on Thermo Scientific Q Exactive UHMR. Prior to Direct Mass Technology mode MS analysis, sample was buffer exchanged into 100 mM ammonium acetate using Zeba spin column (7 kDa MWCO, Thermo Fisher Scientific). Sample was loaded into Au/Pd-coated borosilicate emitters (Thermo Scientific, ES388) for nano-ESI. For Instrument parameters, ion transfer target m/z and detector optimization were set to ‘high m/z.’ In-source trapping was set at −100 V. Trapping gas pressure readout was ~2 × 10−11 mbar. Data were acquired at 200 K @m/z400 resolution setting. Data analysis was done by STORIBoard software (Proteinaceous).
Dodge G.J., Anderson A.J., He Y., Liu W., Viner R, & Imperiali B. (2024). Mapping the architecture of the initiating phosphoglycosyl transferase from S. enterica O-antigen biosynthesis in a liponanoparticle. eLife, 12, RP91125.
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2

Single Ion Mass Spectrometry Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
Single ion measurement using Direct Mass Technology mode was performed on Thermo Scientific™ Q Exactive™ UHMR. Prior to Direct Mass Technology mode MS analysis, sample was buffer exchanged into 100 mM ammonium acetate using Zeba™ spin column (7 kDa MWCO, Thermo Fisher Scientific). Sample was loaded into Au/Pd-coated borosilicate emitters (Thermo Scientific, ES388) for nano-ESI. For Instrument parameters, ion transfer target m/z and detector optimization were set to “high m/z”. In-source trapping was set at −100 V. Trapping gas pressure readout was ~ 2×10−11 mbar. Data were acquired at 200K @m/z400 resolution setting. Data analysis was done by STORIBoard software (Proteinaceous).
Dodge G.J., Anderson A.J., He Y., Liu W., Viner R, & Imperiali B. (2023). Mapping the architecture of the initiating phosphoglycosyl transferase from S. enterica O-antigen biosynthesis in a liponanoparticle. bioRxiv.
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