Mass measurement accuracy of matrix-assisted laser desorbed biomolecules: a Fourier-transform ion cyclotron resonance mass spectrometry study.

The use of binary matrices and internal calibrants to improve the mass measurement accuracy in matrix-assisted laser desorption ionization (MALDI) with Fourier-transform ion cyclotron resonance (FTICR) mass spectrometry is described. Binary matrices enhance the analyte ion yield and enable a complete MALDI-FTICR mass spectrum to be obtained from a single laser shot. The advantage of single-laser-shot data acquisition is that it eliminates line-broadening due to shot-to-shot frequency variations. It is shown that unresolved product ions, mainly due to loss of H2O and/or NH3, shift the centroid of an unresolved multi-component peak. A mass measurement accuracy of 12 ppm was obtained for the bovine insulin [M+H]+ ion using melittin as an internal calibrant.