Advanced Native & Structural Mass Spectrometry Services for Complex Biomolecular Analysis
What we do
The C.T.M. mass-spectrometry laboratory specializes in offering creative structural and native mass-spectrometry solutions for intractable biological and biochemical puzzles, as an advanced high-level scientific service for biotech start-ups, hospitals and academic institutions.
Our Expertise
Advanced mass spectrometry data analysis, experimental design and high-level consulting
High resolution native mass spectrometry of intact large molecules (350 Da and above)
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Top-down fragmentation for extensive biomolecular characterization and analysis
Protein-protein and protein-small molecule Interactions
Our favorite molecules
DNA and RNA oligomers
Synthetic and biological polydisperse polymers
Peptides
soluble and membrane proteins and proteins complexes and their associated small molecules
Cross-linking MS
Membrane Proteins in Detergents
Liposomes and exosomes
Protein complexes in Native Membranes
Our Instruments
Thermo Fisher Q-Exactive UHMR
Thermo Fisher Q-Exactive UHMR (Ultra High Mass Range)- A high- resolution, high-mass, orbitrap based instrument, designed for analysis of large molecules, in their intact and native state. The instrument’s exceedingly high energy output also allows for in-depth analysis of membrane proteins in various mimetic and natural lipid environments.
Thermo Scientific Easy-nLC 1200
A high-performance nanoLC system designed for ultra-sensitive LC–MS analyses. The EASY-nLC 1200 delivers reliable nano-flow chromatography with excellent reproducibility, making it ideal for proteomics and other high-resolution omics applications.
Our Clients
Founders
Dror Chorev, Ph.D.- The laboratory’s chief scientific officer holds a Ph.D. in biochemistry from the Weizmann Institute of Science (IL) and did his post-doctoral training in the University of Oxford (UK). Dror has an extensive, cumulative 15 years experience in mass spectrometry, with IP and 20 peer reviewed works published in high-impact factor journals in the field of native MS.
Selected publications
01.
Lau R.J., Giblin S.P., Sugar A., Di Maio A., Tassini G., Huse K., Chorev D., Chen Y., Wu G.H., Huemer C.B., Seung Kim S.Y., Matthews J., Muloud B., Chen L., McKenna S., Xu Y., Massai L., Muzzi C., Ferhati X., Necchi F., Moriel D.G., Feizi T., Liu Y., Pease J.E., Sriskandan S., and Matthews S.J. SpyCEP dismantles neutrophil immunity via disorder-driven chemokine remodeling and GAG targeting.
02.
Chen S. Getter T., Salom D., Wu D., Quetschlich D., Chorev D.S.,* Palczewski K.,* Robinson C.V*. Capturing a rhodopsin signalling cascade across a native membrane. Nature 604, 384–390 (2022). *Corresponding authors.
03.
Chorev, D.S., and Robinson, C.V. The importance of the membrane for biophysical measurements. Nat Chem Biol 16, 1285–1292 (2020).
04.
Chorev D.S., Tang H., Rouse S.L., Bolla J.R., von Kügelgen A., Baker L.A., Wu D., Gault J., Grünewald K., Bharat A.M.T., Matthews S.J., and Robinson C.V. The use of sonicated lipid vesicles for mass spectrometry. Nat Protoc 15, 1690–1706 (2020).
05.
Chorev, D.S., Baker, L.A., Wu, D., Beilsten-Edmands, V., Rouse, S.L., Zeev-Ben-Mordehai, T., Jiko, C., Samsudin, F., Gerle, C., Khalid, S., et al. (2018). Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry. Science 362, 829-834.
06.
Chorev, D.S., Moscovitz, O., Geiger, B., and Sharon, M. (2014). Regulation of focal adhesion formation by a vinculin-Arp2/3 hybrid complex. Nature communications 5, 3758.
Contact Us
Address
3 Pinkhas Sapir Street
Ness-Tziona, Israel, 7403626