HCTultra ETD II System

Taking the lead in PTM Discovery

Watch the IMSC 2006 presentation "ETD and beyond" in a 14 minute video.

The HCTultra ETD II System™ features ETD: Electron Transfer Dissociation, a fragmentation technique that preserves post-translational modifications . 

Modern functional proteomics demands a step beyond protein identification – it is becoming more and more essential to unravel the many modifications proteins undergo triggering their biological activity.

Unique capabilities for PTM discovery

With ETD, scientists are enabled for specific information-rich PTM (post-translational modifications) analysis on the unsurpassed HCTultra ETD II System™. ETD allows peptide and protein fragmentation while preserving modifications such as phosphorylation or glycosylation. This gives the researcher easy access to protein sequencing and simultaneous identification of type and location of various PTMs.

Proton Transfer Reaction (PTR) is a charge state reduction technique for effective mass range extension

PTR reduces the fragment charge states of multiple charged ETD fragments of intact proteins down to numbers of 2+ to 4+ which can be isotopically resolved in the HCTultra ETD II™ - for optimization of intact protein characterization and top-down PTM characterization.

With ETD, PTR and deconvolution the HCTultra ETD II™ has an effective mass range of >12000 Da.

Powerful de novo sequencing

ETD MS/MS spectra of peptides can now be collected on-the-fly during LC/MS/MS runs using the HCTultra ETD II. Due to its non-ergodic nature, ETD typically creates very clean MS/MS spectra with intact PTMs. On the HCTultra ETD II, the new ETD implementation often provides complete amino acid series, without the low-mass cut-off traditionally encountered in ion trap MS/MS. The combination with the superior mass accuracy of the HCTultra enables powerful de novo sequencing capabilities. Using the PhosphoScan™ mode of the HCTultra with ETD offers a unique and powerful system for single run auto-LC/MS/MS/MS CID/ETD experiments specifically for phosphorylation analysis.

Redefining the Ion Trap standard

The combination of the market-leading acquisition speed and sensitivity of the HCTultra with the new information-rich ETD MS/MS capability redefines ion trap standards for PTM analysis and de novo sequencing – taking the lead, again.

Spherical Ion Trap geometry

In 2005, Bruker Daltonics introduced the first commercial ion trap equipped with ETD, which quickly became the market leader for ETD-ITMS due to the unique advantages of its spherical geometry, which easily traps positive analyte ions and negative ions in the same small spherical volume for maximum ETD interaction efficiency. This spherical trap geometry yields far improved ETD sensitivity, with a factor of 10-100x better sensitivity than ETD in linear ion traps.

• The first commercially available ETD/PTR hardware
• Novel and compact nCI source with increased ETD/PTR reactant generation capabilities.
• Outstanding long term stability
• Outstanding sensitivity
• New Sensitivity spec: Fully automated run, based on 10 fmol BSA digest, short gradient (EASY-nLC: 10 min) and peptide ID via MASCOT.

ETD and PTR are also available as an option for the HCTultra.

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