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The use of the slow crystallisation method to improve matrix‐assisted laser desorption/ionisation time‐of‐flight signals for larger proteins
Author(s) -
Botting Catherine H.
Publication year - 2000
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/1097-0231(20001115)14:21<2030::aid-rcm129>3.0.co;2-3
Subject(s) - chemistry , mass spectrometry , desorption , signal (programming language) , matrix (chemical analysis) , laser , surface enhanced laser desorption/ionization , time of flight mass spectrometry , analytical chemistry (journal) , crystallization , ionization , volume (thermodynamics) , sample (material) , matrix assisted laser desorption/ionization , detection limit , chromatography , optics , adsorption , protein mass spectrometry , tandem mass spectrometry , ion , organic chemistry , physics , computer science , programming language , quantum mechanics
Although matrix‐assisted laser desorption/ionisation time‐of‐flight mass spectrometry uses only a small amount of sample there is a requirement for the sample to be in a concentrated form which can limit the routine use of the technique with larger proteins. The signal from such proteins can also be suppressed by the presence of smaller proteins. Here it is shown that the slow crystallisation method overcomes both these limitations, allowing signals to be obtained from proteins presented at 0.1 pmol/µL and in the presence of smaller contaminants. Signal intensity is volume dependent and spectra can be obtained from crystals prepared in a range of common buffers. Copyright © 2000 John Wiley & Sons, Ltd.