Cryo-EM has rapidly been adopted into drug discovery workflows by the pharmaceutical and biotechnology industries after having proved itself capable of delivering atomic resolution structures for key targets, including integral membrane proteins such as GPCRs and ion channels. More recently, significant improvements in throughput have seen use of the technique expand quickly within the sector. Key to this expansion has been improvements in sample preparation efficiency and reproducibility, which have enabled the investigation of ever more challenging biomolecules.

In this webinar, we will hear from two researchers for whom these new methods were important factors in overcoming sample-specific challenges encountered in structural studies of macromolecules with implications for human health. The presentations will be followed by a roundtable discussion of the role that new sample preparation modalities have played in facilitating these and other drug discovery projects.

Professor Wei-Jen Tang from the University of Chicago uses integrated structural biology techniques such as cryo-EM to elucidate protein-drug interactions, including studies of amyloid peptide-degrading metalloproteases and chemokines involved in neurodegenerative disease. He will speak about his work in overcoming common denaturation effects to determine the cryo-EM structures of multiple states of the relatively small human protein PreP at near atomic resolution.

Radhika Malik is Assistant Professor at the Icahn School of Medicine at Mount Sinai and investigates the structure function relationships of replicating damaged DNA and developing drugs to tackle resulting cancers that prove resilient to conventional chemotherapy. She will present how overcoming strong preferred sample orientation resulted in the first structure of DNA Polζ both in the act of DNA synthesis and without DNA.

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