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Fluorescence-Guided Matrix-assisted Laser Desorption/Ionization with Laser-Induced Postionization Mass Spectrometry of Individual Rat Neural Cells

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Morphology Assessment Enabled by Room-Temperature Soft-Landing in Native MS.

Zihao Qi^1,2, Yu-Fu Lin¹, Sophie R Harvey¹

¹Native MS Guided Structural Biology Center, Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH, 43210, United States.

International Journal of Mass Spectrometry

|June 29, 2026

Summary

Native mass spectrometry combined with room-temperature ion soft-landing prepares protein complexes for electron microscopy. This method aids structural biology research by enabling mass analysis and shape screening of biomolecular assemblies.

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Area of Science:

Structural Biology
Biochemistry
Analytical Chemistry

Background:

Native mass spectrometry (nMS) preserves non-covalent interactions in protein complexes.
Electron microscopy requires well-prepared samples for imaging individual particles.

Purpose of the Study:

To assess native mass spectrometry combined with room-temperature ion soft-landing for preparing protein complexes for electron microscopy.
To evaluate and redesign ion soft-landing setups for compatibility with standard mass spectrometry workflows.

Main Methods:

Utilized native mass spectrometry (nMS) to analyze protein complexes.
Employed room-temperature ion soft-landing to deposit protein complexes onto surfaces.
Performed transmission electron microscopy (TEM) for low-resolution imaging.
Replicated and redesigned ion soft-landing instrumentation for enhanced compatibility.

Main Results:

Successfully landed and imaged two protein complexes (TRAP and VFLIP) with low-resolution TEM, showing agreement with known structures.
Developed a redesigned soft-landing setup that integrates with standard mass spectrometry (MS) instruments (UHMR with ExD-SID), allowing routine nMS experiments without compromising performance.
Demonstrated the compatibility of the redesigned setup with electron capture dissociation (ExD), higher-energy collisional dissociation (HCD), and sustained off-resonance dissociation (SID) fragmentation.

Conclusions:

Room-temperature ion soft-landing is a viable technique for preparing protein complexes for electron microscopy.
The redesigned soft-landing setup facilitates sample preparation and evaluation in early-stage structural biology research.
This integrated approach provides multidimensional information, including mass and shape, for biomolecular assemblies.