Waters - SYNAPT HDMS
Designed for leading researchers working at the limits of conventional mass spectrometry capabilities who need to...
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Features of SYNAPT HDMS
The SYNAPT™ HDMS™ System is a flexible research platform providing:
HDMS mode expands your capabilities beyond conventional MS:
- Triwave™ Technology: Provides access to the unique benefits of ion mobility spectrometry (IMS), conformational studies, reducing sample complexity, and enhanced fragmentation
- Time aligned parallel (TAP) fragmentation: Provides comprehensive structural (MS/MS/MS) information in a single experiment
- High duty cycle (HDC) mode: Enables significant sensitivity enhancements over a wide m/z range
- DriftScope™ Software mobility environment: For interactive visualization and manipulation of multidimensional data
TOF mode for routine qualitative and quantitative exact mass UPLC® /MS/MS:
- Exact mass: 2 ppm RMS
- High resolution: Over 17,500 FWHM
- High sensitivity: Class-leading sensitivity, which features
- Enhanced duty cycle (EDC) capability for maximum duty cycle over specified m/z range
- Dynamic range: > 4 orders of linearity
- UPLC Ready Acquisition Rates: Up to 10 spectra/sec
- Precursor ion selection: 4, 8, and 32KDa quadrupole options for MS/MS analysis
- UPLC/MSE: High-definition metabolite and protein profiling
- MassLynx™ Informatics: i-FIT, MetaboLynx™, MassFRAGMENT™, MarkerLynx™, and ProteinLynx™ Global SERVER
Conformation (IMS) Studies
Measuring the mobility (or drift time) of an ion can yield information about its structure, which you can then use to investigate the size and shape of small and large molecules.
Molecular conformation is critical to the integrity of many biological systems, which means that increased knowledge of the shapes of biologically relevant components (such as proteins, peptides, carbohydrates, and nucleotides) can benefit many research areas.
Analysis of the native and reduced forms of the intact protein Hen Egg Lysosyme using Mobility-TOF (HDMS™) mode on the SYNAPT™ HDMS System. The DrifScope™ Software plot shows m/z versus drift time. Upon acidification and reduction of the native form (single drift time distributions), multiple drift time distributions are observed for the two charge-states shown. This indicates a change in the overall size and shape (topology) of the protein has taken place. Average rotational cross-sections can be determined for the individual conformers from these data.
Modes of Operation
The SYNAPT™ HDMS™ System is a flexible research platform providing both TOF and HDMS modes of operation.
TOF Mode provides application-specific exact mass UPLC® System solutions for your routine qualitative and quantitative applications:
- Proteomics systems: Protein identification, protein quantitation and PTM analysis.
- Small molecule systems: Metabonomics, metabolite identification, impurity profiling, structural elucidation
- Biopharmaceuticals: Peptide mapping, mass confirmation, compound /PTM characterization.
Perform novel ion mobility spectrometry-based investigations in HDMS Mode:
- Separate isobaric components and measure differences in structural conformation
- Remove background and reduce complexity: Increase information content by separating and removing interferences
- Enhanced sequencing and structural characterization with flexible Triwave™ Technology fragmentation protocols, including time-aligned parallel fragmentation.
DriftScope 2.0 Software
Unlock the full power of SYNAPT HDMS
DriftScope™ Mobility Environment Software (v2.0) incorporates new technologies to enable comprehensive retrieval of information contained within HDMS™ (ion mobility) datasets while enabling easier data interpretation (for users of all experience levels) through a series of data visualization and data export enhancements:
- Powerful and automated peak detection (novel APEX 3D and 4D technology)
- Comprehensively reveals all components within any HDMS data (e.g. IMS/MS, LC/IMS/MS and TAP fragmentation) and increases apparent specificity of each analysis
- Eliminates subjectivity from data interpretation, to provide highly reproducible results across analyses and users
Visualization enhancements (e.g. 3D peak profile display, x/y axis switching, peak/raw data overlay, lock-axis function, ability to turn raw data on/off)
- Enables easier and more intuitive data interpretation
- Provides convenient comparison of peaks and supporting raw data
Data export functionality (raw data or peak list export and peak copy/paste function)
- Facilitates data transfer to downstream processing routines
- Streamlines data processing workflows
Enhanced analytical power
- Confident detection of partially (IM) separated compounds (e.g. Isomers or Conformers)
- Visualize new molecular trends in complex mixtures (e.g. crude oil, PEG, MALDI Imaging)
- More efficient characterization with IMS/CID and TAP fragmentation (export of detected peaks directly to MassFragment Software)
Driftscope Mobility Environment Software (version 2.0) provides automated peak detection from 2D (chromatograms and mass spectra) or 3D graphical plots. The axes are interchangeable axes; each pixel represents and ion and its color intensity. The peaks are represented as colored (green) dots and sticks. The data shown is from the Electrospray (infusion-based) IMS-MS analysis of a Polyethylene Glycol (PEG) sample.
Triwave Technology
Triwave™ Technology is the enabling technology behind the SYNAPT™ HDMS™ System. It uses three T-Wave™* ion guides that trap ions, separate them by their ion mobility, and transfer them to the orthogonal acceleration time-of-flight analyzer for high-resolution mass analysis. The trap and transfer regions can also be used for fragmentation analyses.
The Triwave Technology’s innovative configuration overcomes the major performance drawbacks of conventional ion mobility spectrometry (IMS) by ensuring that IMS does not compromise sensitivity.
*The Traveling wave device described here is similar to that described by Kirchner in US Patent 5,206,506; 1993.
Reduce Sample Complexity
The SYNAPT™ HDMS™ System provides a unique way to increase the information content for a variety of applications. DriftScope™ Software eliminates common interferences from an analysis, providing access to lower-level components:
- Separation and removal of interferences; PEG contaminants, chemical noise etc.
- Enhanced detection limits; charge state separation of peptides, PEG, glycans etc.
- Increased information content; structural characterization e.g. Top-Down Proteomics
UPLC® /IMS-TOF sample analysis for rat bile sample containing the dosing vehicle (PEG),
parent drug and its metabolites. The circled regions can be easily removed from the
data set using DriftScope Software (e.g, PEG dosage vehicle).
This provides a simple, unique route to enhanced MS detection of low-level components.
General Specifications
| Mass Range | 20 to 100000 m/z |
| Mass Spectrometer Type | Time-of-Flight |
Additional Specifications
The SYNAPT HDMS System can operator in two modes:
a) TOF mode
b) Mobility-TOF mode
TOF Mass Resolution in Positive Ion
a) V Mode: 10,000 measured on the (M + 6H)^6+ isotope cluster from bovine insulin (m/z 956)
b) W Mode: 17,500 measured on the (M + 6H)^6+ isotope cluster from bovine insulin (m/s 956)
TOF Mass Resolution in Negative Ion
a) V Mode: 10,000 measured on the (M - 4H)^4- isotope cluster from bovine insulin (m/z 1431)
b) W Mode: 17,500 measured on the (M - 4H)^4- isotope cluster from bovine insulin (m/z 1431)
Positive Ion MS Sensitivity
a) V Mode: The peak at m/z 556 from a solution of 50 pg/µL leucine enkephalin in 50/50 acetonitrile/water + 0.1% formic acid, infused at a flow rate of 5 µL/min, will have an intensity of greater than 1,700 counts per second. The instrument will be tuned to 10,000 resolution (as demonstrated on bovine insulin) and the mass range will be set to 1,000 Da.
b) EDC: The peak at m/z 556 from a solution of 10 pg/µL leucine enkephalin in 50/50 acetonitrile/water + 0.1% formic acid, infused at a flow rate of 5 µL/min, will have an intensity of greater than 2,000 counts per second. The instrument will be tuned to 10,000 resolution (as demonstrated on bovine insulin), with sensitivity set to a maximum at 556 Da.
Negative Ion MS Sensitivity:
V Mode: The peak at m/z 503 from a solution of 500 pg/µL raffinose in 70/30 acetonitrile/water (no additives), infused at a flow rate of 5 µL/min, will have an intensity of greater than 1,800 counts per second. The instrument will be tuned to 10,000 resolution (as demonstrated on bovine insulin), and the mass range will be set to 1,000 Da.
Positivt Ion MS/MS Sensitivity
V Mode: Using a [Glu]-Fibrinopeptide B solution of 100 fmol/µL, at a flow rate of 5 µL/min and with the instrument tuned for 10,000 resolution (as demonstrated on bovine insulin), the intensity of the most intense y" sequence ion from the MS/MS spectrum of the doubly charged precursor ion (785.8 Da) will be greater than 130 counts per second. This will correspond to a signal to noise ratio of greater than 50:1 (after a 3x9 smooth) on the most intense y" sequence ion, for a 1 second scan. The instrument mass range will be set to 2,000 Da.
Negative Ion MS/MS Sensitivity
V Mode: Using a solution of 500 pg/µL raffinose in 70/30 acetonitrile/water, at a flow rate of 5 µL/min and with the instrument tuned for 10,000 resolution (as demonstrated on bovine insulin), the intensity of the fragment ion at 179.1 Da in the MS/MS spectrum of the precursor ion at 503.2 Da will be greater than 130 counts per second. The instrument mass range will be set to 1,000 Da.
Mass Scale Calibration Accuracy
The mass measurement accuracy of the instrument in V-mode, using an internal lockmass, is such that the RMS error between the measured and the accepted masses of peaks which have sufficient intensity, and are free from interference from other masses, will be less than 2 ppm over the range of 150-900 Da.
Mass Measurement Accuracy
The mass measurement accuracy of the instrument, in W-mode, will be better than 2 ppm RMS, based on 10 consecutive repeat measurements of the [M + Na]^+ ion of raffinose (m/z 527.1588), using the [M + H]^+ ion of leucine enkephalic (556.2771) as the LockSpray lockmass. Analyte lockmass peaks must have sufficient intensity and be free of interference from other masses.
Mass Range
The TOF mass range is 20 - 100,000 Da in V-mode, and 20 - 26,500 Da in W-mode.
The quadrupole mass range in non-resolving mode is 20 - 16,000 Da for a 4,000 Da quadrupole, and 20 - 32,000 Da for an 8,000 Da quadrupole.
See PDF for further specifications.