Thermo Scientific™ Orbitrap Fusion™ Tribrid™ Mass Spectrometer by Thermo Fisher Scientific

"It opens new directions on my environmental metabolic analyses"

"High resolution, good for a variety of studies, easy interface,"

"The Fusion is as comprehensive an instrument as available giving the ability to use multiple ionization techniques with improved throughput, sensitivity and monitoring over previous instruments in this category."

"MS remains the most powerful technique to study the glycosylation and glycan types in glycoproteins. The most useful bottom-up method to characterize the glycosylation on glycoproteins is to analyze the intact glycopeptides using LC-MS/MS. This workflow has advantage that it allows to direct analyze the information of the glycans correlated to their attachment sites in the protein(s). One main determinant of these glycoprotein profiling approaches is the mass spectrometry techniques used, including the resolution of the MS, dissociation techniques and data acquiring speed. There are several dissociation ways to generate MS/MS and MSn data, and the most common ones are collision-induced dissociation (CID), higher energy collisional dissociation (HCD), electron capture dissociation (ECD) and electron transfer dissociation (ETD). ETD is the most widely used one and is highly orthogonal to CID in analyzing glycopeptides. For intact glycopeptides MS/MS analysis, CID has limitations that cannot yield extensive peptide backbone fragmentation and cannot yield the information about modification site due to the labile nature of the glycan attachment to the peptide ion. However, CID can generate fragment ions from cleavage of glycosidic bonds that can be used to elucidate oligosaccharide sequence. In contrast to CID, ETD dissociation occurs at peptide linkages rather than at glycosidic linkages, which preserves labile glycosylated linkages and allows the identification of the glycopeptide as well as the assignment of its glycosylation sites. The MS technique is keeping on development and the performance of MS plays important role for intact glycopeptides analysis. In this Orbitrap hybrid mass spectrometer, the precursor is selected using the quadrupole mass filter and the ion trap and Orbitrap analyzers can operate in parallel, which could improve the acquisition speed to 18 to 20 Hz. It has been well proved that the new quadrupole/linear ion trap/Orbitrap tribrid mass spectrometer (Q-OT-qIT, Orbitrap Fusion) can improve the proteome coverage and peptide identification rates."

"The Fusion Mass Spec is everything in one package. Allows simultaneous series or parallel experiments with very good resolution and sensitivity while allowing the monitoring of several ions. It has great workflow and through put for complex proteome scanning allowing for faster assays and discovery."

"The Fusion Lumos system is really easy to use and to carry out daily maintenance, making it robust and reliable to perform a broad spectrum of quantitative mass spectrometry analyses."

"Good sensitivity and resolution for SILAC analysis"

"This is an excellent instrument."

"The machine is good for ID and SILAC ratio for cell signaling research. "