Product category:
Mass spectrometers
News Release from: Waters | Subject: Synapt HDMS System
Edited by the Laboratorytalk Editorial
Team on 20 March 2007
Synapt HDMS mass spectrometry on show at
Pittcon
The Synapt HDMS System is intended for researchers working at the limits of conventional mass spectrometry (MS) and who need to further characterise and define their samples
The Synapt HDMS system is the first mass spectrometer of its kind to employ high efficiency ion-mobility based measurements and separations and specialised software to enable the analysis of sample ions differentiated by size, shape and charge as well as mass This additional dimension of separations fidelity leads to improved specificity and sample definition, meaning scientists can extract more information about their samples including the detection of previously unseen constituents
This article was originally published on Laboratorytalk on 7 Jun 2006 at 8.00am (UK)
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A technological first for mass spectrometry
Synapt HDMS is the first mass spectrometer of its kind to employ new ion-mobility technology and software to enable the analysis of sample ions differentiated by size and shape, as well as mass
A key feature of this new system is the patented Waters Triwave technology, a unique method for combining high efficiency, ionmobility-based measurements and separations with high performance quadrupole, time-of-flight mass spectrometry.
Visualization and manipulation of the multi-dimension data produced by the system is performed by DriftScope Mobility Environment software, while operational control is provided by Waters MassLynx software.
Earlier this year, Waters announced that the world-renowned Max Planck Institute is enhancing its research on neurodegenerative diseases by adding a Waters Synapt High Definition MS (HDMS) System to its complement of research technologies.
Further reading
High definition mass spec is first of its kind
Synapt HDMS system is the first mass spectrometer of its kind to employ new ion mobility technology and software to enable the analysis of sample ions differentiated by size, charge, shape and mass.
Redefining molecular characterisation science
Waters highlighted new mass spectrometry, proteomics and software innovations focused on characterising and visualising molecules at the 55th annual American Society for Mass Spectrometry, 3-7 June
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The Institute's Department of Cellular Biochemistry recently took delivery of the Synapt HDMS System to study the role of proteins in causing brain-wasting diseases such as Huntington's Disease.
"Our initial impression of the Synapt HDMS system was of a very powerful two-dimensional separation device.
"We wanted a system that could measure large intact protein complexes with high accuracy.
"The ability to additionally separate species by ion mobility greatly enhances the appeal of this system," commented Max Planck Institute director and professor Ulrich Hartl, and Manajit Hayer-Hartl, principal investigator.
Dr Hayer-Hartl's research focuses on the understanding of the mechanisms by which molecular chaperones mediate protein folding and inhibit misfolding in neurodegenerative diseases.
The Synapt System will analyse the large protein complexes, and their subunit composition, that are involved in such diseases.
Hartl and Hayer-Hartl are looking to the Synapt system to give them greater insight into protein folding, assembly, and aggregation pathways by being able to resolve, identify and characterise intermediates based on differences in conformation, something that is nearly impossible to do with current technology.
Oxford University is another Synapt HDMS customer.
The instrument will be used by the Department of Chemistry to study interactions between proteins and small molecules as well as interactions between proteins and other bio-macromolecules.
"We are particularly keen to apply the capability of the Synapt HDMS System to separate species by ion mobility," commented Chris Schofield of the Department of Chemistry.
"We hope it will enable us to study the effects of binding events on protein conformation in an efficient manner and complement data obtained from high resolution but time consuming techniques such as X-ray crystallography and NMR.
"Obtaining three-dimensional information on proteins is difficult to do by existing mass spectrometric-based techniques".
Shipments of the new mass spectrometer commenced in December of 2006.
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