Protein complexes were buffer exchanged in 0.5 M NH4OAc buffer (pH 6.9) using VIVASPIN 50-kDa MWCO filters (Fisher Scientific, Hanover Park, IL). The final concentration of protein complexes was adjusted to 10 μM. A 10-μl aliquot was loaded into an offline electrospray capillary (Thermo Electron, Madison, WI) to perform the Native-MS measurement on an Exactive Plus EMR mass spectrometer (Thermo Fisher Scientific, Bremen, Germany). The sample solution was infused in positive mode at capillary voltage 1.5–1.8 kV to the instrument with the resolving power set at 17,500. The in-source and HCD collision voltages were adjusted for desolvation of the ions. The instrument was calibrated with the clusters produced by ESI of a CsI solution. The peak picking and data processing was performed with Intact Mass software (Protein Metrics, San Carlos, CA).
Vivaspin 50 kda mwco filters
Manufactured by Thermo Fisher Scientific
The VIVASPIN 50-kDa MWCO filters are centrifugal concentrators used for the separation and concentration of macromolecules such as proteins, enzymes, and nucleic acids. These filters have a molecular weight cut-off (MWCO) of 50 kDa, allowing the retention of molecules above this size while allowing smaller molecules to pass through.
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2 protocols using vivaspin 50 kda mwco filters
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Native Mass Spectrometry of Protein Complexes
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Native Mass Spectrometry of Protein Complexes
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Protein complexes were buffer exchanged in 0.5 M NH4OAc buffer (pH 6.9) using VIVASPIN 50-kDa MWCO filters (Fisher Scientific, Hanover Park, IL). The final concentration of protein complexes was adjusted to 10 μM. A 10-μl aliquot was loaded into an offline electrospray capillary (Thermo Electron, Madison, WI) to perform the Native-MS measurement on an Exactive Plus EMR mass spectrometer (Thermo Fisher Scientific, Bremen, Germany). The sample solution was infused in positive mode at capillary voltage 1.5–1.8 kV to the instrument with the resolving power set at 17,500. The in-source and HCD collision voltages were adjusted for desolvation of the ions. The instrument was calibrated with the clusters produced by ESI of a CsI solution. The peak picking and data processing was performed with Intact Mass software (Protein Metrics, San Carlos, CA).
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