<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Snyder DT</submitter><funding>National Institutes of Health</funding><funding>NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>116503</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8057730</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>461</volume><pubmed_abstract>We describe instrumentation for conducting tandem surface-induced dissociation (tSID) of native protein complexes on an ultrahigh resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer. The two stages of SID are accomplished with split lenses replacing the entrance lenses of the quadrupole mass filter (stage 1, referred to herein as SID-Q) and the collision cell (stage 2, Q-SID). After SID-Q, the scattered projectile ions and subcomplexes formed in transit traverse the 20 mm pre-filter prior to the mass-selecting quadrupole, providing preliminary insights into the SID fragmentation kinetics of noncovalent protein complexes. The isolated SID fragments (subcomplexes) are then fragmented by SID in the collision cell entrance lens (Q-SID), generating subcomplexes of su</pubmed_abstract><journal>International journal of mass spectrometry</journal><pubmed_title>Tandem surface-induced dissociation of protein complexes on an ultrahigh resolution platform.</pubmed_title><pmcid>PMC8057730</pmcid><funding_grant_id>S10 OD018507</funding_grant_id><funding_grant_id>P41GM128577</funding_grant_id><funding_grant_id>R01 GM120425</funding_grant_id><funding_grant_id>P41 GM128577</funding_grant_id><pubmed_authors>Wysocki V</pubmed_authors><pubmed_authors>Snyder DT</pubmed_authors><pubmed_authors>Lin YF</pubmed_authors><pubmed_authors>Somogyi A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Tandem surface-induced dissociation of protein complexes on an ultrahigh resolution platform.</name><description>We describe instrumentation for conducting tandem surface-induced dissociation (tSID) of native protein complexes on an ultrahigh resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer. The two stages of SID are accomplished with split lenses replacing the entrance lenses of the quadrupole mass filter (stage 1, referred to herein as SID-Q) and the collision cell (stage 2, Q-SID). After SID-Q, the scattered projectile ions and subcomplexes formed in transit traverse the 20 mm pre-filter prior to the mass-selecting quadrupole, providing preliminary insights into the SID fragmentation kinetics of noncovalent protein complexes. The isolated SID fragments (subcomplexes) are then fragmented by SID in the collision cell entrance lens (Q-SID), generating subcomplexes of su</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Mar</publication><modification>2026-03-18T13:16:21.048Z</modification><creation>2025-04-04T19:58:22.996Z</creation></dates><accession>S-EPMC8057730</accession><cross_references><pubmed>33889055</pubmed><doi>10.1016/j.ijms.2020.116503</doi></cross_references></HashMap>