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A calibration routine for efficient ETD in large-scale proteomics
Journal article   Open access

A calibration routine for efficient ETD in large-scale proteomics

Christopher M Rose, Matthew J P Rush, Nicholas M Riley, Anna E Merrill, Nicholas W Kwiecien, Dustin D Holden, Christopher Mullen, Michael S Westphall and Joshua J Coon
Journal of the American Society for Mass Spectrometry, Vol.26(11), pp.1848-1857
11/2015
DOI: 10.1007/s13361-015-1183-1
PMCID: PMC5642106
PMID: 26111518
url
http://doi.org/10.1007/s13361-015-1183-1View
Open Access

Abstract

Electron transfer dissociation (ETD) has been broadly adopted and is now available on a variety of commercial mass spectrometers. Unlike collisional activation techniques, optimal performance of ETD requires considerable user knowledge and input. ETD reaction duration is one key parameter that can greatly influence spectral quality and overall experiment outcome. We describe a calibration routine that determines the correct number of reagent anions necessary to reach a defined ETD reaction rate. Implementation of this automated calibration routine on two hybrid Orbitrap platforms illustrate considerable advantages, namely, increased product ion yield with concomitant reduction in scan rates netting up to 75% more unique peptide identifications in a shotgun experiment. Graphical Abstract ᅟ.
Tandem Mass Spectrometry - standards Peptides - chemistry Proteomics - standards Calibration Kinetics Proteomics - methods Tandem Mass Spectrometry - methods Peptides - analysis

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