Top down proteomics by EAD!

While I am skeptical of the currently accepted machanism for how those magnets induce electron activated dissociation (EAD), it's a super cool new technology. ETD but with basically no reaction time and no scary reagents?  Wins all around.

In this newest application of the technology these authors apply it to top down proteomics

They mix up some commercial histone standards and show they can resolve and identify their PTM sites, then they do some bigger proteins (heavy chain might be the biggest protein they try in the paper) and then also resolve some intact glycosylated proteoforms.

I thought this was a neat trick for overriding the default limiter for the ZenoPulsing (for the shotgun proteomics methods it was designed for you're more worried about saturating the detectors than what happens if your signal is a little lower, which is a very different problem than for intact proteins that really really don't want to fly). 

My very first question was "cool, but what can process these files?" and they used OpenMS and Flash Deconvolv (something like that? I might have the name partially mixed up with another similar thing and I'm not going back to the paper to look it up - definitely had Flash in the title). I'm pretty sure that if you can master the OpenMS framework that thing can process basically anything and this supports that assumption.