A Cryogenic-Temperature Ion Mobility Mass Spectrometer for Improved Ion Mobility Resolution

2010 ◽  
pp. 137-151 ◽  
Author(s):  
Jody May ◽  
David Russell
2018 ◽  
Vol 17 (12) ◽  
pp. 2534-2545 ◽  
Author(s):  
Florian Meier ◽  
Andreas-David Brunner ◽  
Scarlet Koch ◽  
Heiner Koch ◽  
Markus Lubeck ◽  
...  

2013 ◽  
Vol 85 (19) ◽  
pp. 9003-9012 ◽  
Author(s):  
Alexey A. Sysoev ◽  
Denis M. Chernyshev ◽  
Sergey S. Poteshin ◽  
Alexander V. Karpov ◽  
Oleg I. Fomin ◽  
...  

2009 ◽  
Vol 81 (2) ◽  
pp. 618-624 ◽  
Author(s):  
Francisco A. Fernandez-Lima ◽  
Christopher Becker ◽  
Kent J. Gillig ◽  
William K. Russell ◽  
Shane E. Tichy ◽  
...  

2015 ◽  
Vol 7 (3) ◽  
pp. 863-869 ◽  
Author(s):  
R. Fernandez-Maestre ◽  
C. Wu ◽  
H. H. Hill

We introduced methanol into the buffer gas of an ion mobility spectrometer-mass spectrometer and mobilities changed depending on ion structures; baseline separation of valine, asparagine, and tetraalkylammonium ions was achieved.


2019 ◽  
Author(s):  
Dorte B. Bekker-Jensen ◽  
Ana Martínez del Val ◽  
Sophia Steigerwald ◽  
Patrick Rüther ◽  
Kyle Fort ◽  
...  

ABSTRACTState-of-the-art proteomics-grade mass spectrometers can measure peptide precursors and their fragments with ppm mass accuracy at sequencing speeds of tens of peptides per second with attomolar sensitivity. Here we describe a compact and robust quadrupole-orbitrap mass spectrometer equipped with a front-end High Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) Interface. The performance of the Orbitrap Exploris 480 mass spectrometer is evaluated in data-dependent acquisition (DDA) and data-independent acquisition (DIA) modes in combination with FAIMS. We demonstrate that different compensation voltages (CVs) for FAIMS are optimal for DDA and DIA, respectively. Combining DIA with FAIMS using single CVs, the instrument surpasses 2500 unique peptides identified per minute. This enables quantification of >5000 proteins with short online LC gradients delivered by the Evosep One LC system allowing acquisition of 60 samples per day. The raw sensitivity of the instrument is evaluated by analyzing 5 ng of a HeLa digest from which >1000 proteins were reproducibly identified with 5 minute LC gradients using DIA-FAIMS. To demonstrate the versatility of the instrument we recorded an organ-wide map of proteome expression across 12 rat tissues quantified by tandem mass tags and label-free quantification using DIA with FAIMS to a depth of >10,000 proteins.


2009 ◽  
Vol 287 (1-3) ◽  
pp. 46-57 ◽  
Author(s):  
Paul R. Kemper ◽  
Nicholas F. Dupuis ◽  
Michael T. Bowers

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