Scientists must look beyond studying individual proteins and examine the structure and assembly of protein complexes within cells in order to truly understand how proteins function in their native environment. Combining cryo-electron microscopy (cryo-EM) with the advances in mass spectrometry (MS) have had a considerable impact on structural biology research, enabling researchers to characterize biomolecular structures with greater speed, sensitivity and selectivity.

In this webinar, Dr. Pascal Albanese discusses the characterization of a key enzyme of the central carbon metabolism of Pyrococcus furious through an integrative approach that combines structural mass spectrometry, cryo-electron microscopy, mass photometry, and molecular modelling with molecular dynamics simulations. He also describes how his lab unveiled the structural organization of phosphoenolpyruvate synthase (PPSA).

Learning objectives:

  • Discover the value of using cryo-EM to understand protein structure and function
  • Discuss insights gained by incorporating crosslinking reagents with MS analysis
  • Explain the importance of standardized sample preparation to establish robust end-to-end workflow solutions

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