The Thermo Scientific Tundra Cryo-Transmission Electron Microscope (Cryo-TEM) is a dedicated structure-determination solution designed to bring single particle analysis to every biochemistry laboratory. It is easier to use than typical cryo-TEM instruments, fits into a standard lab space, and matches grant mechanisms and funding opportunities globally. The Tundra Cryo-TEM is a powerful tool that can help answer your most challenging research questions, offering structural determination at biologically relevant resolutions.
Structural information at biologically relevant resolution
The optics of the Tundra Cryo-TEM are specifically designed so that you can answer fundamental questions on biology and human disease with data at biologically relevant resolutions. Our first and only microscope operating at 100 kV, the Tundra Cryo-TEM can generate high-contrast biological images at medium throughput with its high-performance, fraction-enabled Thermo Scientific Ceta Camera.
This special combination of optics and detector technology enables the Tundra Cryo-TEM to solve protein structures to biologically relevant resolution at medium throughput.
Space efficient and cost effective
The new hardware architecture of the Tundra Cryo-TEM has been purposefully designed with a smaller footprint and an easier access path without sacrificing performance. In many cases, this allows you to avoid the additional investment and unwanted downtime that comes with modification of your existing laboratory infrastructure (or even the need for a new, purposely built lab) to accommodate the instrument.
Additionally, a wide range of funding and instrumentation grants were considered when designing the Tundra Cryo-TEM so that its price falls within the reach of most instrumentation grants.
Easy, iterative sample-viability determination and biochemistry optimization
Electron microscopy is a straightforward method for the quality assessment of purified biological specimens at the microscopic scale. The Tundra Cryo-TEM can visualize the impact of biochemical adjustments to samples faster than other technologies, since you do not need to go through the lengthy process of crystals growth.
Each iteration is extremely efficient due to the instrument’s sample loading technology. It only takes a few minutes to exchange samples in and out of the microscope, allowing you to optimize sample conditions quickly. Notably, this technology is designed so that even new users are capable of doing this procedure without extensive training. The instantaneous feedback of the Tundra Cryo-TEM significantly shortens the time required for biochemical sample optimization.
Unique AI algorithms
The Tundra Cryo-TEM comes with a complete suite of automation software for efficient optimization of your sample's biochemistry as well as data collection for structural determination. This includes user-friendly single particle analysis (SPA) data acquisition software, Thermo Scientific EPU 2 Software, guided day-to-day operation, a traffic-light UI element that indicates the microscope’s status, and pre-defined templates for typical use cases that allow you to begin collecting high-resolution data with only a few clicks.
Additionally, the Tundra Cryo-TEM is the debut of smart EPU software, an AI-enabled software solution capable of analyzing intermediate results, providing instant feedback, and steering data collection on the fly. Our AI algorithms are based on years of cryo-EM knowledge, replace decisions that experts need to make upfront, and ensure that your instrument is working at optimal conditions, allowing you to focus on the science rather than on fine-tuning the microscope.
3D structures answer your biological questions
One of the primary challenges of investigating dynamic biological processes, and how they fail in disease, is the complexity inherent to biological machinery. Large and/or dynamic protein systems present a unique challenge to traditional methods of scientific inquiry, which study these systems either indirectly or in isolation. Fortunately, cryo-electron microscopy (cryo-EM) single particle analysis (SPA) has emerged as a well-suited approach for the direct determination of native function and dynamics in complex biological systems.
Single particle analysis can validate your biochemistry work by showing the molecular details that underlie the interactions between proteins, small molecules, and post-translational modifications in large and dynamic protein systems at near native conditions. These molecular details confirm the mechanism of action by which complex biological systems (e.g. membrane proteins, protein complexes, and macromolecular machines such as viruses, ribosomes, and proteasomes) contribute to human health and disease.
For example, the human GABAA (gamma-aminobutyric acid type A) receptor is a small membrane protein and ligand-gated chloride-ion channel that mediates inhibitory neurotransmission. GABAA receptors are important therapeutic targets as their various conformations affect a variety of important signaling pathways. Due to GABAA's conformational flexibility, traditional methods have been unable to reveal its molecular mechanism of action. The ability of cryo-EM to image large, biologically complex structures has, meanwhile, allowed researchers to see the molecular details that underpin the allosteric modulation of this important receptor.
With the Tundra Cryo-TEM, more scientists can have access to this type of information for their complex biological systems. Our applications scientists have used the Tundra Cryo-TEM to determine a 3D structure of GABAA to ~4-5 Å resolution. At this resolution, molecular details such as individual alpha helices and beta sheets are clearly visible, molecular structures can be docked, and molecular interactions modeled. Additionally, the Tundra Cryo-TEM was able to achieve 3 Å resolution for the rigid benchmark protein apoferritin. At this resolution, the protein backbone can be traced and major amino acid side chains are clearly visible, making de novo model building possible. Data at these resolutions helps you understand how proteins function, how to modify genes, and how to design drugs accordingly.
Technical highlights of the Tundra Cryo-TEM
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Floor-plan and installation requirements
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Learn about the latest biological research conducted using the new Tundra Cryo-TEM, find out how it’s democratizing cryo-electron microscopy, and engage with our experts and guest speakers during the panel discussion.
Get ready for game-changing access to cryo-EM and see how greater structural insights can solve the most difficult protein structures at the heart of our greatest medical challenges. This will, in turn, help us gain insight into diseases that we have only just begun to understand.
Learn about the latest biological research conducted using the new Tundra Cryo-TEM, find out how it’s democratizing cryo-electron microscopy, and engage with our experts and guest speakers during the panel discussion.
Get ready for game-changing access to cryo-EM and see how greater structural insights can solve the most difficult protein structures at the heart of our greatest medical challenges. This will, in turn, help us gain insight into diseases that we have only just begun to understand.
Infectious Disease Research
Cryo-EM techniques enable multiscale observations of 3D biological structures in their near-native states, informing faster, more efficient development of therapeutics.
Structural Biology Research
Cryo-electron microscopy enables the structural analysis of challenging biological targets such as large complexes, flexible species and membrane protein.
Single Particle Analysis
Single particle analysis (SPA) is a cryo-electron microscopy technique that enables structural characterization at near-atomic resolutions, unraveling dynamic biological processes and the structure of biomolecular complexes/assemblies.
Single Particle Analysis
Single particle analysis (SPA) is a cryo-electron microscopy technique that enables structural characterization at near-atomic resolutions, unraveling dynamic biological processes and the structure of biomolecular complexes/assemblies.
