LMB / Science / Facilities / Mass Spectrometry
Caterina Franco

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Facilities

Mass Spectrometry

The Mass Spectrometry facility supports three main areas of mass spectrometry: quantitative proteomics, structural proteomics and intact mass determination.

Woman in a lab coat and purple gloves meticulously works on a sample at a bench in a lab with other researchers and equipment.
The Mass Spectrometry facility team in action, hard at work behind the scenes.

Quantitative proteomics uses mass spectrometry to identify and quantify proteins in highly complex samples such as tissues and cells. The set of proteins in a cell together with their modifications and interactions, provides a rich assessment of cell function at any given time. By tracking the proteome of living systems under various conditions, LMB researchers gain insights into how cells and organisms respond to physiologic perturbations, stress, disease progression, drug treatments and much more.

Quantitative proteomic pipelines in the facility include a Thermo Orbitrap Eclipse, a Thermo Orbitrap QExactive Classic and a Thermo Orbitrap QExactive Plus.

Woman in lab coat and purple gloves inserts a component into a large piece of scientific equipment with blue accents and green lights.
Mass spectrometer weekly maintenance to ensure smooth operation and reliable performance.

Structural proteomics uses hydrogen-deuterium exchange mass spectrometry (HDX-MS) and protein crosslinking mass spectrometry (CL-MS) to study protein structures and interactions. This work is supported by a Thermo Orbitrap Ascend, a Thermo Orbitrap QExactive HFx with a Waters HDX manager and a custom-designed UV cross-linking workstation.

Intact mass determination using Thermo Orbitrap Exploris MX and a Bruker MALDI-TOF/TOF helps users to validate many of their synthetic or protein purification projects by ensuring their proteins have the expected post-translational modifications or providing a quick intact mass assessment of their native complexes.

Selected Publications

KIF1C activates and extends dynein movement through the FHF cargo adapter.Abid Ali F, Zwetsloot AJ, Stone CE, Morgan TE, Wademan RF, Carter AP, Straube ANat Struct Mol Biol 32(4): 756-766 (2025)
Co-opting templated aggregation to degrade pathogenic tau assemblies and improve motor function.Miller LVC, Papa G, Vaysburd M, Cheng S, Sweeney PW, Smith A, Franco C, Katsinelos T, Huang M, Sanford SAI, Benn J, Farnsworth J, Higginson K, Joyner H, McEwan WA, James LCCell 187(21): 5967-5980.e17 (2024)
Mechanism of orphan subunit recognition during assembly quality control.Yagita Y, Zavodszky E, Peak-Chew SY, Hegde RSCell 186(16): 3443-3459.e24 (2023)
Mechanism of ribosome-associated mRNA degradation during tubulin autoregulation.Höpfler M, Absmeier E, Peak-Chew SY, Vartholomaiou E, Passmore LA, Gasic I, Hegde RSMol Cell 83(13): 2290-2302.e13 (2023)