PXD062360 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Understanding m/z range settings for MS/MS scans: a case study with intact glycopeptides |
| Description | Several practical considerations dictate the scan range, or breadth of ion m/z values, that can be transmitted through ion guides in mass spectrometers (MS). Voltage settings must be balanced to minimize low m/z cutoffs while also generating effective pseudopotential wells for high m/z ions to maximize transmission of ion populations of interest. The scan range is particularly impactful in glycoproteomics, because glycopeptide identification typically relies on low mass-to-charge (m/z) glycan-derived oxonium ions and higher m/z peptide fragments that retain glycan modifications. Common practice suggests a so-called “5-10-15 rule” when setting scan ranges, which defines the upper m/z value to be used for the scan based on a multiple of the first m/z value. While this axiom has very real implications for transmitting diverse ion populations in full MS scans, adhering to this strategy can unnecessarily limit analytical information available in glycopeptide MS/MS spectra. Here, we explore the implications of following or breaking the 5-10-15 rule in MS/MS scans for glycopeptide characterization on a quadrupole-Orbitrap-linear ion trap Tribrid MS system (Orbitrap Ascend). We show that breaking the 5-10-15 rule does not lead to a significant loss of fragment ion transmission at either extreme of the m/z range. We demonstrate this concept for glycopeptides fragmented with higher-energy collisional dissociation (HCD), electron-transfer dissociation (ETD), and electron-transfer/higher-energy collision dissociation (EThcD). We use this case study to discuss the concepts important to using the 5-10-15 rule wisely and when it can be practically ignored, such as using large m/z ranges to improve glycopeptide characterization. |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-06-08 |
| AnnouncementXML | Submission_2026-06-07_16:10:59.607.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Tim S Veth |
| SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606; |
| ModificationList | complex glycosylation |
| Instrument | Orbitrap Ascend |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2025-03-28 13:31:31 | ID requested | |
| ⏵ 1 | 2026-06-07 16:11:00 | announced | |
Publication List
| 10.1021/jasms.5c00352; |
| Veth TS, Kothlow K, Riley NM, Range Settings for MS/MS Scans: A Case Study with Intact Glycopeptides. J Am Soc Mass Spectrom, 37(4):872-883(2026) [pubmed] |
Keyword List
| submitter keyword: glycobiology, glycopeptides,Mass spectrometry, mass range |
Contact List
| Nicholas M. Riley |
| contact affiliation | University of Washington, Department Chemistry, Seattle, WA, 98195 |
| contact email | nmriley@uw.edu |
| lab head | |
| Tim S Veth |
| contact affiliation | University of Washington |
| contact email | tveth@uw.edu |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
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| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD062360
- Label: PRIDE project
- Name: Understanding m/z range settings for MS/MS scans: a case study with intact glycopeptides