Document Detail


An automated high performance capillary liquid chromatography-Fourier transform ion cyclotron resonance mass spectrometer for high-throughput proteomics.
MedLine Citation:
PMID:  14766289     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We describe a fully automated high performance liquid chromatography 9.4 tesla Fourier transform ion resonance cyclotron (FTICR) mass spectrometer system designed for proteomics research. A synergistic suite of ion introduction and manipulation technologies were developed and integrated as a high-performance front-end to a commercial Bruker Daltonics FTICR instrument. The developments incorporated included a dual-ESI-emitter ion source; a dual-channel electrodynamic ion funnel; tandem quadrupoles for collisional cooling and focusing, ion selection, and ion accumulation, and served to significantly improve the sensitivity, dynamic range, and mass measurement accuracy of the mass spectrometer. In addition, a novel technique for accumulating ions in the ICR cell was developed that improved both resolution and mass measurement accuracy. A new calibration methodology is also described where calibrant ions are introduced and controlled via a separate channel of the dual-channel ion funnel, allowing calibrant species to be introduced to sample spectra on a real-time basis, if needed. We also report on overall instrument automation developments that facilitate high-throughput and unattended operation. These included an automated version of the previously reported very high resolution, high pressure reversed phase gradient capillary liquid chromatography (LC) system as the separations component. A commercial autosampler was integrated to facilitate 24 h/day operation. Unattended operation of the instrument revealed exceptional overall performance: Reproducibility (1-5% deviation in uncorrected elution times), repeatability (<20% deviation in detected abundances for more abundant peptides from the same aliquot analyzed a few weeks apart), and robustness (high-throughput operation for 5 months without significant downtime). When combined with modulated-ion-energy gated trapping, the dynamic calibration of FTICR mass spectra provided decreased mass measurement errors for peptide identifications in conjunction with high resolution capillary LC separations over a dynamic range of peptide peak intensities for each spectrum of 10(3), and >10(5) for peptide abundances in the overall separation.
Authors:
Mikhail E Belov; Gordon A Anderson; Mark A Wingerd; Harold R Udseth; Keqi Tang; David C Prior; Kenneth R Swanson; Michael A Buschbach; Eric F Strittmatter; Ronald J Moore; Richard D Smith
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Journal of the American Society for Mass Spectrometry     Volume:  15     ISSN:  1044-0305     ISO Abbreviation:  J. Am. Soc. Mass Spectrom.     Publication Date:  2004 Feb 
Date Detail:
Created Date:  2004-02-09     Completed Date:  2004-04-21     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9010412     Medline TA:  J Am Soc Mass Spectrom     Country:  United States    
Other Details:
Languages:  eng     Pagination:  212-32     Citation Subset:  IM    
Affiliation:
Biological Sciences Division and Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Automation
Chromatography, High Pressure Liquid
Cyclotrons
Deinococcus / chemistry,  cytology
Electrophoresis, Capillary
Fourier Analysis
Mass Spectrometry / instrumentation*,  methods*
Molecular Sequence Data
Peptides / analysis*,  chemistry
Proteomics / instrumentation,  methods*
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical
Reg. No./Substance:
0/Peptides

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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