The Thermo Scientific Vitrobot Mark IV System offers semi-automated vitrification to provide fast, easy, and reproducible sample preparation for cryo-EM. It performs the cryo-fixation process at constant physical and mechanical conditions like temperature, relative humidity, blotting conditions, and freezing velocity. This ensures high-quality cryo-fixation results and a high sample preparation throughput prior to cryo-TEM observation.
The Vitrobot System offers great value to the demanding scientific areas of cell biology and molecular imaging. It is equally suitable for food, industrial, pharmaceutical, and nanotechnological applications - where the true colloidal structure of your analyte is critical.
Highly automated vitrification process with enclosed process chamber:
Vitrobot Mark IV System provides precise and flexible control of all critical parameters in the plunge-freezing process:
Easy and flexible user interface:
The Vitrobot Mark IV System is compatible with multiple sample types, such as proteins, bacteria, and cells to fulfill your multiple structural biology applications requirements.
Learn how to use the Vitrobot Mark IV System from preparing the system to vitrifying a sample with these step-by-step videos.
Weight | 31 kg |
Dimensions | L/W/H: 413/260/890 mm |
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Find relevant citations from peer-reviewed journals where specific research results were generated using the Vitrobot Mark IV System.
Cryo-EM grid optimization for membrane proteins
Kampjut D, Steiner J & Sazanov LA. Cryo-EM grid optimisation for membrane proteins. iScience : 102139 (2021).
https://doi.org/10.1016/j.isci.2021.102139
Structure deformation and curvature sensing of PIEZO1 in lipid membranes
Yang, X., Lin, C., Chen, X. et al. Structure deformation and curvature sensing of PIEZO1 in lipid membranes. Nature 604, 377–383 (2022).
https://doi.org/10.1038/s41586-022-04574-8
Integrative structure of a 10-megadalton eukaryotic pyruvate dehydrogenase complex from native cell extracts.
Kyrilis FL, Semchonok DA, Skalidis I, et al. Integrative structure of a 10-megadalton eukaryotic pyruvate dehydrogenase complex from native cell extracts. Cell Reports 34 (2021).
https://doi.org/10.1016/j.celrep.2021.108727
Dynamics of GLP-1R peptide agonist engagement are correlated with kinetics of G protein activation.
Deganutti, G., Liang, YL., Zhang, X. et al. Dynamics of GLP-1R peptide agonist engagement are correlated with kinetics of G protein activation. Nat Commun 13, 92 (2022).
https://doi.org/10.1038/s41467-021-27760-0
Structural basis of actin filament assembly and aging
Oosterheert, W., Klink, B.U., Belyy, A. et al. Structural basis of actin filament assembly and aging. Nature 611, 374–379 (2022).
For Research Use Only. Not for use in diagnostic procedures.