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Speaker: Dr Basil Greber, Division of Structural Biology, The Institute of Cancer Research
Host: Julien Bergeron
In recent years, technological developments in cryo-electron microscopy have revolutionised structural biology. I will briefly introduce some of these developments using my previous work on ribosomal complexes as an example. Subsequently, I will discuss how these technologies have enabled the structure determination of human transcription factor IIH, a multifunctional protein machine whose components play important roles in transcription initiation, DNA repair, and the regulation of cyclin-dependent kinases. This work led to new insight into the architecture of the complex and the control of its constituent enzymatic subunits. In the last part of my talk, I will summarize my most recent work on the structure of the human CDK-activating kinase, a sub-complex of TFIIH that is a promising target for development of cancer therapeutics. This work involved structure determination of a 85 kDa protein module to 2.5 Å resolution, making it one of the smallest asymmetric complexes resolved at this level of detail using cryo-EM.
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