A high‐resolution scanning microprobe matrix‐assisted laser desorption/ionization ion source for imaging analysis on an ion trap/Fourier transform ion cyclotron resonance mass spectrometer
- 25 September 2008
- journal article
- research article
- Published by Wiley in Rapid Communications in Mass Spectrometry
- Vol. 22 (20) , 3275-3285
- https://doi.org/10.1002/rcm.3733
Abstract
A new scanning microprobe matrix‐assisted laser desorption/ionization (SMALDI) ion source for high spatial resolution has been developed for linear ion trap and Fourier transform ion cyclotron resonance mass spectrometry (FT‐ICR‐MS). The source is fully compatible with commercial ion trap flanges (such as the LTQ series, Thermo Fisher Scientific). The source is designed for atmospheric pressure (AP) operation but is also suitable for mid‐pressure operation. The AP mode is especially useful for investigating volatile compounds. The source can be interchanged with other ion sources within a minute when operated in the AP mode. Combining high‐lateral resolution MALDI imaging with high mass resolution and high mass accuracy mass spectrometry, available in the FT‐ICR mode, provides a new quality of analytical information, e.g. from biological samples. First results obtained with the new ion source demonstrate a maximum lateral resolution of 0.6 by 0.5 µm. Depending on the limit of detection of the chosen mass analyzer, however, the size of the focus had to be enlarged to a diameter of up to 8 µm in the FT‐ICR mode, in order to create enough ions for detection. Mass spectra acquired for analytical imaging were obtained from single laser pulses per pixel in all the experiments. This mode allows us to investigate biological thin sections with desorption focus diameters in the micrometer range, known to cause complete evaporation of material under the laser focus with a very limited number of laser pulses. As a first example, peptide samples deposited in microstructures were investigated with the new setup. A high quality and validity of the acquired images were obtained in the ion trap mode due to the low limit of detection. High mass resolution and accuracy but poorer image quality were obtained in the ICR mode due to the lower detection sensitivity of the ICR detector. Copyright © 2008 John Wiley & Sons, Ltd.Keywords
This publication has 36 references indexed in Scilit:
- Identification of proteins directly from tissue: in situ tryptic digestions coupled with imaging mass spectrometryJournal of Mass Spectrometry, 2007
- Functional and topological characterization of protein interaction networksProteomics, 2004
- Oligomerization and substrate binding studies of the adenylate kinase from Sulfolobus acidocaldarius by matrix-assisted laser desorption/ionization mass spectrometryThe Analyst, 2000
- Investigations of 2,5-DHB and succinic acid as matrices for UV and IR MALDI. Part II: Crystallographic and mass spectrometric analysisInternational Journal of Mass Spectrometry and Ion Processes, 1997
- Influence of the laser intensity and spot size on the desorption of molecules and ions in matrix-assisted laser desorption/ionization with a uniform beam profileInternational Journal of Mass Spectrometry and Ion Processes, 1995
- Dynamical parameters of ion ejection and ion formation in matrix- assisted laser desorption/ionizationEuropean Journal of Mass Spectrometry, 1995
- Factors affecting the resolution in matrix-assisted laser desorption—ionization mass spectrometryInternational Journal of Mass Spectrometry and Ion Processes, 1994
- α‐Cyano‐4‐hydroxycinnamic acid as a matrix for matrixassisted laser desorption mass spectromtryJournal of Mass Spectrometry, 1992
- Cinnamic acid derivatives as matrices for ultraviolet laser desorption mass spectrometry of proteinsRapid Communications in Mass Spectrometry, 1989
- Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltonsAnalytical Chemistry, 1988