TY - JOUR
T1 - Mass correlated acceleration in a reflectron MALDI TOF mass spectrometer
T2 - An approach for enhanced resolution over a broad mass range
AU - Kovtoun, Slava V.
AU - English, Robert D.
AU - Cotter, Robert J.
N1 - Funding Information:
The authors are grateful to Suzanne M. Ramirez for her initial assistance in the protein digest and cleanup procedures. This work was supported by the Defense Advanced Research Project Agency (DARPA) (Grant DABT63-99-1-0006).
PY - 2002
Y1 - 2002
N2 - Compared to continuous extraction, pulsed extraction (PE) of ions formed by matrix-assisted laser desorption/ionization (MALDI) in time-of-flight (TOF) mass spectrometers significantly improves mass resolution. Parameters such as extraction voltage, delay time, and correction pulse must be varied, however, to achieve optimum mass resolution over a broad mass range because the PE method is mass dependent. We previously reported a novel method, mass correlated acceleration (MCA), which we have now combined with a reflectron MALDI TOF mass spectrometer to further enhance mass resolution over a broader mass range. Unlike the PE method, MCA is not mass dependent and high resolution mass spectra can be achieved with a single tuning of instrument parameters. The ions may be brought into focus simultaneously, i.e., the multi-channel recording advantage can be more fully realized. The MCA dual-stage ion source design includes an extraction pulse region and an acceleration region that contains a time-dependent waveform correlated with mass. We demonstrate the validity of this novel technique with applications in peptide mixture analysis and protein digests of lysozyme and bovine serum albumin.
AB - Compared to continuous extraction, pulsed extraction (PE) of ions formed by matrix-assisted laser desorption/ionization (MALDI) in time-of-flight (TOF) mass spectrometers significantly improves mass resolution. Parameters such as extraction voltage, delay time, and correction pulse must be varied, however, to achieve optimum mass resolution over a broad mass range because the PE method is mass dependent. We previously reported a novel method, mass correlated acceleration (MCA), which we have now combined with a reflectron MALDI TOF mass spectrometer to further enhance mass resolution over a broader mass range. Unlike the PE method, MCA is not mass dependent and high resolution mass spectra can be achieved with a single tuning of instrument parameters. The ions may be brought into focus simultaneously, i.e., the multi-channel recording advantage can be more fully realized. The MCA dual-stage ion source design includes an extraction pulse region and an acceleration region that contains a time-dependent waveform correlated with mass. We demonstrate the validity of this novel technique with applications in peptide mixture analysis and protein digests of lysozyme and bovine serum albumin.
UR - http://www.scopus.com/inward/record.url?scp=0036099408&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036099408&partnerID=8YFLogxK
U2 - 10.1016/S1044-0305(01)00346-4
DO - 10.1016/S1044-0305(01)00346-4
M3 - Article
C2 - 11838017
AN - SCOPUS:0036099408
SN - 1044-0305
VL - 13
SP - 135
EP - 143
JO - Journal of the American Society for Mass Spectrometry
JF - Journal of the American Society for Mass Spectrometry
IS - 2
ER -