Mass spectrometry analyses were performed as described previously (Cartier-Michaud et al., 2017) . Raw files generated from mass spectrometry analysis were processed with Proteome Discoverer 1.4 (Thermo Fisher Scientific), searching data via in-house Mascot server (version 2.4.1; Matrix Science Inc., London, UK) against the B. subtilis database (4300 references) of the Swissprot database (version 2020.04). For the database search, the following settings were used: a maximum of one miscleavage, oxidation as a variable modification of methionine, carbamidomethylation as a fixed modification of cysteine and trypsin was set as the enzyme. A peptide mass tolerance of 6 ppm and a fragment mass tolerance of 0.8 Da was used for search analysis. Only peptides with high stringency identity Mascot score (false discovery rate (FDR)<1%) were used for protein identification.
Mascot server version
Manufactured by Matrix Science
Sourced in United Kingdom
The Mascot server is a powerful software solution developed by Matrix Science for the analysis of mass spectrometry data. It serves as a core component in the identification and characterization of proteins from complex biological samples. The Mascot server provides a robust and reliable platform for processing and interpreting mass spectrometry data, enabling researchers to gain valuable insights into the composition and structure of proteins.
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Lab products found in correlation
2 protocols using mascot server version
1
Mass Spectrometry of B. subtilis Proteome
2
E. coli Proteome Profiling by LC-MS/MS
Check if the same lab product or an alternative is used in the 5 most similar protocols
Escherichia coli protein extracts were digested with trypsin and analysed by LC‐MS/MS following the protocol described by Sang et al. (2018 ). The mass spectra were submitted to Mascot Server (version 2.5.1, Matrix Science, London, UK) for peptide identification and searched against the E. coli protein database supplemented with GFP protein sequence and flagellin protein sequences from P. syringae and R. solanacerum.
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Escherichia coli protein extracts were digested with trypsin and analysed by LC‐MS/MS following the protocol described by Sang et al. (
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