Fresh colony yeast was applied directly to a sample plate of the equipment, the samples were coated with a saturated solution of α-cyano acid 4-hydroxy cinnamic diluted in 50% ACN with 2.5% TFA. The Mass spectra were recorded using a MALDI-TOF MS Autoflex Speed (Bruker Daltonics, Bremen, Germany) equipped with an intelligent beam laser source (334 nm). The analyses were analyzed in linear mode with positive polarity, acceleration voltage of 20 kV and delay extraction of 220 ns. Each spectrum was collected as an average of 1200 laser shots with enough energy to produce good spectra without saturation in the range of m/z from 2000 to 20,000. Before analysis, the equipment was externally calibrated with the protein calibration standard I (Bruker Daltonics, Bremen, Germany, insulin, ubiquitin, cytochrome C and myoglobin) with FlexControl 1.4 software (Bruker Daltonics, Bremen, Germany). The analyses were analyzed with the MALDI Biotyper Compass 4.1 software (Bruker Daltonics, Bremen, Germany) in the range of m/z 3000–15,000 compared with a library of 1301 spectra of fungal identifications.
Flexcontrol 1
Manufactured by Bruker
Sourced in Germany
FlexControl 1.4 is a software suite developed by Bruker for the control and operation of their analytical instruments. It provides a user-friendly interface to manage and monitor the instrument's various functions and parameters. The software is designed to work seamlessly with Bruker's hardware offerings, enabling efficient and reliable data acquisition and processing.
Automatically generated - may contain errors
4 protocols using flexcontrol 1
1
MALDI-TOF MS for Fungal Identification
2
Yeast Colony MALDI-TOF-MS Identification
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Samples of yeast were incubated in the dark at 37 °C for 48 h, then colony samples were applied directly to a sample plate of the equipment, following the procedures as described by Gobom et al., 2011 [34 (link)], where the sample was coated with a saturated solution of α-cyano acid 4-hydroxy cinnamic diluted in 50% ACN with 2.5% TFA. The mass spectra were used using a MALDI-TOF-MS Autoflex Speed (Bruker Daltonics, Bremen, Germany) equipped with an intelligent beam laser source (334 nm). Analysis was carried out in the linear mode with positive polarity, an acceleration voltage of 20 kV and a delay extraction of 220 ns. Each spectrum was collected as an average of 1200 laser shots with enough energy to produce good spectra without saturation in the range of m/z from 2000 to 20,000. Before analysis, the equipment was externally calibrated with the protein calibration standard I (Bruker Daltonics, Bremen, Germany; insulin, ubiquitin, cytochrome C and myoglobin) with FlexControl 1.4 software (Bruker Daltonics, Bremen, Germany). Analysis was carried out with the MALDI Biotyper Compass 4.1 software (Bruker Daltonics, Bremen, Germany) in the range of m/z 3000–15,000 compared to a library of 1301 spectra of fungal identifications.
3
Acyl-ACP Purification and Mass Spectrometry
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BioH reaction mixtures (20 μl) were loaded onto Vivapure D Mini H columns (Sartorius Stedim) which were washed twice with loading buffer (25 mM sodium MES, 10 mM DTT, pH 6.1) containing 250 mM LiCl. Acyl-ACPs were eluted with same buffer containing 500 mM LiCl followed by dialysis against 200 mM ammonium acetate overnight at 4 °C using a 3,500 molecular weight cut-off membrane. The samples were dried under a nitrogen stream53 (link). Mass spectral analyses were performed by the University of Illinois Mass Spectrometry Laboratory. The mass spectra were collected under low resolution in positive ion mode on an UltrafleXtreme MALDI TOF/TOF mass spectrometer (Bruker Daltonics, Bremen, Germany) equipped with a frequency tripled Nd–YAG solid state laser using the FlexControl 1.4 software package (Bruker Daltonics).
4
Purification and Analysis of Acyl-ACP Derivatives
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The solutions of acyl-ACP derivatives from the reconstituted assays described above were loaded in binding buffer (25 mM 4-morpholineethanesulfonic acid, pH 6.1) containing 100 mM LiCl and the column was washed twice with the same buffer containing 250 mM LiCl. Acyl-ACPs were eluted in binding buffer containing 500 mM LiCl followed by dialysis using a 3,500 molecular weight cut-off membrane against 2 mM ammonium acetate at 4 °C for 15 h. The extracts were dried under a stream of nitrogen and 2 μg samples were dissolved in 20 μl 50% acetonitrile containing 0.1% formic acid. Mass spectral analyses were performed by the University of Illinois Mass Spectrometry Laboratory. The mass spectra were collected in positive ion mode on an UltrafleXtreme MALDI TOF/TOF mass spectrometer (Bruker Daltonics) equipped with a frequency tripled Nd–YAG solid state laser using the FlexControl 1.4 software package (Bruker Daltonics). Following external calibration, 2000 spectra were acquired at 500 Hz using a randomized raster, summed, and saved for analysis. Data processing was done using the FlexAnalysis 3.4 software package (Bruker Daltonics). Spectra were smoothed and a baseline correction was applied using the software package features.
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