As a reversible retrofit, the ExD Option has been integrated into a wide variety of platforms. Be sure to check out all of the new research featuring e-MSion ExD at ASMS in the abstract list below!



We are pleased to be hosting the first ExD for Q Exactive user meeting for current and prospective customers at this year’s ASMS, in partnership with Zef Scientific.

Join us for lunch to hear the latest from current users and to find out more about the future of ExD from e-MSion’s technical team!


Amanda Helms
Brodbelt Lab
University of Texas at Austin
Multiple Methods for Dissociation and Their Application on the UHMR
Won Jung, Ph.D.
Gupta Lab
Yale Medical School
Native Top-Down Analysis of Membrane Proteins Directly from the Lipid Bilayer
Kelly Gallagher, Ph.D.
Heck Lab
Utrecht University
The Application of ECD for De Novo Sequencing of Antibodies
Carter Lantz
Loo Lab
University of California Los Angeles
Native Top-Down Mass Spectrometry with Electron-based Dissociation on an Orbitrap-based Instrument Reveals Sequence and Structure Information for Native Proteins and Protein Complexes
Chen Du
Wysocki Lab
The Ohio State University
A Hybrid ECD-SID Device Enhances Top-Down and Structural Characterization of Native Protein Complexes


Extend the capability of your Thermo Scientific Q Exactive mass spectrometer to include electron-based fragmentation with e-MSion’s ExD cell. Now supported and serviced by Zef Scientific.

The affordable electron capture dissociation (ECD) upgrade enables innovative top-down (Figure 1), middle-down, and native workflows for comprehensive characterization of protein sequence, posttranslational modifications, and higher-order structure.

Adding ECD to your workflow is easier than ever before with our new data analysis and visualization software, ExDViewer (Figure 2). See the results for yourself and explore our interactive web demo at


Figure 1: Coverage map showing ECD of Carbonic Anhydrase II (25+) obtained by direct infusion using the ExD TQ-160 Option for Thermo Scientific Q Exactive MS.


Figure 2: Screenshot of ExDViewer software, e-MSion’s new ECD data analysis and visualization solution.


Learn more about the TQ-160 Option for Thermo Scientific Q Exactive MS at or contact ZefSci at





MS Vision is an independent technology and services company providing value-added services and upgrade paths for mass spectrometry technology. MS Vision currently operates out of offices in the UK, Netherlands and Germany. As a vendor-independent service provider, MS Vision has extensive experience in high-mass and native electrospray mass spectrometry—which is why e-MSion is excited to announce we’re joining forces with MS Vision by entering into a multiyear sales and support agreement. MS Vision is our distribution and support partner for e-MSion in the European Union, United Kingdom, Switzerland and Norway.

ECD technology has traditionally been implemented only on high-end mass spectrometry systems such as FT-ICR-MS making it available for only a few specialized labs. Our mission is to advance mass spectrometry-based life sciences research by offering accessible electron-capture dissociation (ECD) fragmentation. The new and complementary data enabled by our ExD technology unlocks new avenues of protein characterization that will be of value to drug manufacturers and academic researchers alike.

When combined with MS Vision high-mass technology, the e-MSion ExD technology provides a practical solution for top-down biomolecule analysis on your current instruments. MS Vision will sell and support e-MSion’s ExD packages as upgrades for existing Waters Synapt and Thermo Fisher Q Exactive systems, in addition to servicing upgraded systems for customers all over Europe.

Upgrading to ExD means increased capabilities for your instruments and clearer results for your team. This includes:

  • Seamless integration with existing instrument hardware
  • Retention of labile post-translational modifications
  • Sequencing of larger peptides and intact proteins

Be sure to visit our website at for more information on our ExD technology and its applications. For questions regarding ECD or high-mass upgrades on your existing instruments as well as general service-related inquiries please visit or send an email to

Follow us on LinkedIn for more updates on ExD technology!

On March 24, 2020, Dr. Liangliang Sun and Ph.D. candidate Xiaojing Shen from the Department of Chemistry at Michigan State University shared their research on the separation and top-down characterization of proteoforms and protein complexes, both native and denatured, using capillary electrophoresis-mass spectrometry (CEMS) and a combination of ECD and CID (“ECciD”).

Since December 2019, Dr. Sun has been an early adopter of e-MSion ExD technology. Here, Sun and Shen discuss using an e-MSion ExD cell on an Agilent 6545XT AdvanceBioTM LC/Q-TOF to obtain extensive sequence coverage of proteins smaller than 30 kDa following separation by CE. They also describe how predicting the electrophoretic mobility of proteoforms can be used to increase confidence of proteoform IDs.

To watch the webinar, click here.

The Sun group also recently presented their work with CEMS and ECD at the 68th annual ASMS conference. Check out Xiaojing Shen’s poster: Improving CZE-MS/MS for both denatured and native top-down proteomics (ThP 544).

ASMS 2020 Reboot conference attendees can view all abstracts, posters, and oral presentations through the online portal until August 31st. Afterwards, members can find conference proceedings through the ASMS website.

On June 24th, 2:30 to 3:15 EST, Dr. Ruotolo from the Department of Chemistry at University of Michigan will speak on the advances made in collision induced unfolding (CIU) methods as part of an Agilent-hosted discussion on new tools for biotherapeutic characterization.

To register for the webinar, click here.

Agilent announces the immediate availability of the ExD AQ-250​ Option, which provides a new, powerful, and easy-to-use electron-based fragmentation technology that is a field-installed enhancement for the 6545-6560 family of Q-TOFs. The e-MSion ExD AQ-250​ Option makes possible far more complete characterization of proteins and glycoproteins with unprecedented accuracy, speed and simplicity. The ExD AQ-250​ Option is comarketed with e-MSion Inc located in Corvallis, Oregon. The technology has been developed through a ten-year collaborative effort with Agilent.

The ExD AQ-250​ Option is available for both new Agilent instruments or can be retrofitted into recent existing Q-TOF mass spectrometers. The ExD AQ-250​ Option is a drop-in replacement for the Agilent collision cell that offers superior electron fragmentation in combination with collision induced dissociation (CID) to produce more reliable identification of larger peptides and proteins than previously possible. The original functionality, sensitivity, and resolution of the Q-TOF are preserved and the ExD can be automatically optimized with Agilent’s SWARM optimization.

The ExD cell is the only electron-based technology that fast enough to fragment proteins after with ion mobility separation (IMS). When installed on Agilent’s 6560 Ion Mobility Q-Tof, the ExD AQ-250​ Option gives provides unprecedented and unique abilities to probe protein conformation after separation by ion mobility.

e-MSion’s ExD technology fragments proteins in precise and predictable ways in common with electron transfer dissociation (ETD). ExD fragmentation is simpler because no trapping is needed with a negatively charged ETD reagent. The major advantage of ExD over ETD is the ability to activate analyte ions before, during and after electron capture using CID. As a result, the ExD cell produces higher coverage of native proteins up to 25-30 kDa than possible with other commercially available fragmentation techniques and with more simplicity.

Unlike ETD, the ExD technology can produce higher energy electrons to fragment across more complex ring structures to give better characterization of glycans. In addition, ExD induces side chain fragmentation that can differentiate isobaric leucine from isoleucine, and to provide better mapping disulfide chains. The ExD cell also readily distinguishes isoaspartate from aspartate and other degradation products affecting biopharmaceutical quality.

The ExD technology preserves labile post-translational modifications on large peptides and intact proteins, which allows for the simultaneous quantitation of multiple phosphorylation and glycation sites in bottom-up and middle down proteomic work flows.

The superior dissociation of native proteins by ExD with retention of post-translational modifications and side chain differentiation opens new opportunities for more complete characterization of complex proteoforms in a highly cost-effective platform.


Oregon State University has announced that the 16th Uppsala Conference on Electron-Based Fragmentation has been postponed until 2021. The following notice has been released by OSU:


Due to the growing uncertainty of the impact of COVID-19 a decision has been made to postpone this event. We regret to inform you that the 16th Uppsala Conference on Electron-Based Fragmentation, hosted at Oregon State University has been postponed until 2021. We will add further information as it develops. If you have questions please contact Conference Services at We thank you in advance for your patience during a time of high communications volume with our team.


The conference was originally scheduled to take place from August 9th-12th, including an optional Oregon Coast Excursion to conclude the event. Sponsors include e-MSion, Agilent, and OSU. For more information and updates, click here to visit the official page for UPPCON 2021.