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What’s New in MS Structure ID Suite Version 2021

Version 2021 of MS Structure ID Suite adds new features, including automated structure identification, and improves existing ones. Read below for details, and contact us for help upgrading your software.

  • We improved data import from:
    • Shimadzu LabSolutions CDS—you can now import data via the Connect to External Application dialog box or the ACD/Labs/Shimadzu LabSolutions CDS Add-on
    • Agilent OpenLab CDS—you can now select a whole folder or several files to import at once, via the Connect to External Application dialog box or the Add-on
    • Thermo Chromeleon—you can now import LC/MS data, via the Connect to External Application dialog box or the Add-on

Automatically Identify Unknown Components by Mass Search

  • The new Automated MS Structure ID tool automatically finds candidate structures for unknown components based on spectral mass
    • You can choose to search for every component in the dataset or for a selected mass
    • The best hit (based on mass difference and Auto Assignment of predicted fragments) is automatically placed in the Table of Components. You can manually select a different candidate from the Table of Search Results.
    • Find the tool by right-clicking the Table of Components or by going to Tools > Automated MS Structure ID

Display Fragment Structures as Peak Annotations

  • You can now annotate peaks with their associated fragment structures. This works with fragment structures assigned manually or via Auto Assignment.
    • Fragment annotations are also displayed in database records and on reports
    • Find this option, and adjust structure size and style, in the MS Preferences or LC/UV/MS Preferences dialog box

      Fragment structures appear above the corresponding peaks in the mass spectrum

Record and Automate Frequent Actions

  • Record automatic and manual processing actions for LC/UV/MS data in the Recording Log. Stop and start recording by clicking Recording in the toolbar or by using the Recording Log dialog box.
  • Automate actions by generating a script from actions saved in the Recording Log

Access More Features by Converting Flat Chromatograms into Hyphenated Data

  • Turn flat (single-channel) chromatograms into hyphenated data to access Projects and the Table of Components. Now single-channel and multi-dimensional datasets will have a consistent look.
    • This option automatically appears during data import. It can also be activated manually under Tools > Convert to Hyphenated Data.
    • Previously, single-channel chromatograms could only be imported as flat chromatograms, which don’t support features like the Table of Components

Get Better Results from Automatic Processing with IntelliXtract 2.0 and IXCR 2.0

  • You can now set an Abundance Threshold for components to be identified via spectral search
  • Auto Interpret Component Spectrum now gives more accurate adduct labels. We added checks for adduct pairs like [M+NH3+H]+. We also improved annotation of multiply charged ions and multimers.
  • You can now see the retention time difference (tR Difference) between experimental and reference chromatograms in the Table of Components
  • We made spectral search faster

Improve Processing with More Tools and Options

  • You can now match peaks between chromatograms in an LC/MS series. Both manual and automatic matching are available. Previously, peak matching was only available between datasets opened in separate windows (not in series mode).
  • Subtract one DAD (diode array detector, LC/UV) dataset from another. For example, you can correct a sample chromatogram and spectrum by blank subtraction.
  • We improved the peak detection algorithm, and added the Baseline Liftoff and Baseline Touchdown options, so you can refine the integration by moving the start and end points of the peak
  • Generate formulae for multiple m/z values within a mass spectrum, while setting individual parameters for each mass range
    • Select m/z values for formula generation by specifying the Abundance Threshold (%)
    • Define mass ranges, and set the types and numbers of atoms for each range
  • You can now annotate spectra with fragment losses (e.g., loss of HCl)

Filter MS Searches by Polarity

  • When searching databases by spectra, the search now returns only reference spectra with the same polarity as the query

Improved search for structures that include graphical objects, molecules with chiral centers, and data range values

  • Search for large/complex molecules where graphical objects are used to represent defined formulas

    Represent complex molecules with graphical objects, e.g., proteins, antibody-drug conjugates, nanoparticles on surfaces, etc
  • Improved search for structures that contain chiral atoms with “&” and “or” enhanced stereo labels (where “&” denotes a racemic center and “or” denotes relative configuration). Previously the labels provided incomplete/incorrect search results.

    Improved search for structures that contain chiral atoms with “&” and “or” enhanced stereo labels

In the search query, “or” labels indicate a search for the same relative chiral center configuration.

An exact search returns C and D as results. A and B are not returned since they have absolute stereo configuration, not relative. E is not returned because the centers have different relative configurations.

In a substructure search, only F–I are returned as results because those structures (can) have the same relative configuration as the query. J is not returned because it has a different relative configuration.

  • Search results of ranged values are more reproducible (e.g., when searching for compounds with a melting point of 65°C, record sets with the following in the melting point field will now be returned: 50-100°C, <100°C, >50°C)

Features for Other Techniques

As always, you can process data from other analytical techniques in MS Structure ID. We’ve improved features for these techniques as well:

Analysis of NMR Data with MS Structure ID

Define Co-existing Rotamers in NMR Spectra

  • You can now define and report co-existing rotamers. Select the rotamer peaks in your spectrum and identify them as rotamers. You can then adjust the proton ratios with 0.1H accuracy

    In the above structure, rotation around the amide bond is restricted, leading to 2 rotamers being formed. By defining H3a protons as doublets, you can adjust their proton ratios to sum to 1. This functionality is found in the Multiplet Analysis dialog box.
1H NMR (DMSO-d6) δ: 8.47 (d, J=7.0 Hz, 0.4H rotamer), 8.18 (d, J=7.0 Hz, 0.6H rotamer)

Report multiplet results for samples containing rotamers in US patent format, or create customized reports in most other formats.

Unfold Folded 2D Spectra to Get the True Position of Peaks

  • You can now unfold folded 2D spectra along the F1 axis to reveal the correct positions of peaks

    Left: overlaid HMBC (red) and HSQC (green) spectra of azithromycin. The signals from HMBC appearing at ~0 ppm in 13C belong to folded peaks. Their true position is greater than the HMBC upper F1 range. Apply process-correct aliased frequencies to adjust the spectrum along F1 range. After unfolding, the signals appear at their correct position around 220ppm (right).

Integrate All Peaks in Series of NMR Data

  • In Group mode, view peak integral values for all spectra in a series

    A series of 1D 1H NMR spectra for ethylindanone. In group mode, you can display and selectively position the integral values for all peaks in the series.