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New design for a time-of-flight mass spectrometer with a liquid beam laser desorption ion source for the analysis of biomolecules

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4 Author(s)
Charvat, A. ; MPI für Biophysikalische Chemie, Am Fassberg 11, D-37077 GöttingenInstitut für Physikalische Chemie, Universität Göttingen, Tammannstrasse 6, D-37077 Göttingen, Germany ; Lugovoj, E. ; Faubel, M. ; Abel, B.

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We describe a novel liquid beam mass spectrometer, based on a recently discovered nanosecond laser desorption phenomenon, [W. Kleinekofort, J. Avdiev, and B. Brutschy, Int. J. Mass Ion. Processes 152, 135 (1996)] which allows the liquid-to-vacuum transfer, and subsequent mass analysis of pre-existing ions and ionic associates from liquid microjets of aqueous solutions. The goal of our novel technical approach is to establish a system with good mass resolution that implements improvements on critical components that make the system more reliable and easier to operate. For laser desorption pulsed dye-laser difference frequency mixing is used that provides tunable infrared light near the absorption maximum of liquid water around 3 μm. Different types of liquid beam glass nozzles (convergent capillary and aperture plate nozzles) are investigated and characterized. Starting from theoretical considerations of hydrodynamic drag forces on micrometer size droplets in supersonic rarefied gas flows we succeeded in capturing efficiently the liquid beam in a liquid beam recycling trap operating at the vapor pressure of liquid water. For improving the pollution resistance, the liquid jet high vacuum ion source region is spatially separated from the reflectron time-of-flight mass spectrometer (TOF–MS) working behind a gate valve in an ultrahigh vacuum environment. A simple (simulation optimized) ion optics is employed for the ion transfer from the source to the high vacuum region. This new feature is also mostly responsible for the improved mass resolution. With the present tandem-TOF–MS setup a resolution of m/Δm≈1800 for the low and m/Δm≈700 in the high mass region has been obtained for several biomolecules of different mass and complexity (amino acids, insulin, and cytochrome c). © 2004 American Institute of Physics.

Published in:

Review of Scientific Instruments  (Volume:75 ,  Issue: 5 )