CryoEM analysis of small plant biocatalysts at sub-2 Å resolution

Nicole Dimos, Carl P.O. Helmer, Andrea M. Chánique, Markus C. Wahl, Robert Kourist, Tarek Hilal, Bernhard Loll

Research output: Contribution to journalArticlepeer-review


Enzyme catalysis has emerged as a key technology for developing efficient, sustainable processes in the chemical, biotechnological and pharmaceutical industries. Plants provide large and diverse pools of biosynthetic enzymes that facilitate complex reactions, such as the formation of intricate terpene carbon skeletons, with exquisite specificity. High-resolution structural analysis of these enzymes is crucial in order to understand their mechanisms and modulate their properties by targeted engineering. Although cryo-electron microscopy (cryoEM) has revolutionized structural biology, its applicability to high-resolution structural analysis of comparatively small enzymes has so far been largely unexplored. Here, it is shown that cryoEM can reveal the structures of plant borneol dehydrogenases of ∼120 kDa at or below 2 Å resolution, paving the way for the rapid development of new biocatalysts that can provide access to bioactive terpenes and terpenoids.

Original languageEnglish
Pages (from-to)113-123
Number of pages11
JournalActa Crystallographica Section D : Structural Biology
Publication statusPublished - 1 Jan 2022


  • borneol dehydrogenases
  • camphor
  • cryo-electron microscopy
  • green chemistry
  • high resolution
  • plant biocatalysts
  • terpenes

ASJC Scopus subject areas

  • Structural Biology


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