Webinar

Join us for a presentation from Dr. Basil Greber, Team Leader, ICR, as he describes how the new Glacios 2 Cryo-TEM is facilitating the discovery of next-generation cancer therapeutics. To learn more about our next generation Glacios 2 Cryo-TEM, watch our complementary launch event now on-demand.

On-demand Webinar: Introducing Glacios 2 Cryo-TEM- High-resolution structure determination tool with unparalleled automation and ease of use

Webinar Live Date: 5 October, 2022
Duration: 17 minutes

Introducing Glacios 2 Cryo-TEM: High-resolution structure determination tool with unparalleled automation and ease of use

During this event, we unveiled the new Thermo Scientific Glacios 2 Cryo-Transmission Electron Microscope, which delivers higher throughput, creates higher-resolution structures, and features an improved interface that’s easier to use. In addition, we shared an overview of the Glacios 2 Cryo-TEM, presented ground-breaking data collected with the instrument, shared a testimonial from one of our collaborators, and answered some of your questions.

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On-demand Presentation: Harnessing the power of cryo-EM for discovery of cancer therapeutics- High-resolution structures of the human CDK-activating kinase bound to inhibitors

Presentation Live Date: 18 October, 2022
Duration: 40 minutes

Dr. Basil Greber from the Institute of Cancer Research in London, UK, demonstrated how the Glacios 2 Cryo-TEM facilitated the discovery of next-generation therapeutics. 

Dr. Greber and his team used the Glacios 2 Cryo-TEM in their efforts to make CDK-activating kinase (CAK) amenable to structure-based drug design. First, they determined the structures of the human CAK bound to nucleotide analogues and two inhibitors. They then used the Glacios 2 Cryo-TEM equipped with a Thermo Scientific Selectris X Imaging Filter and a Thermo Scientific Falcon 4i Direct Electron Detector to uncover the structural basis of inhibitor selectivity, which required rapid acquisition of high-quality datasets for large numbers of different inhibitors.

This workflow enabled 3D reconstruction of the CAK at 3.5 to 4.5 Å resolution within one hour from the start of data collection and at approximately 3 Å resolution within four hours. Finally, they obtained more than a dozen high-resolution structures of the 85 kDa CDK-cyclin-module of the human CAK bound to inhibitors and nucleotides at up to 1.8 Å resolution using a Thermo Scientific Krios G4 Cryo-TEM with a cold-FEG. These structures provided detailed insight into inhibitor binding and suggested a mechanism for target selectivity that they are currently testing.

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