Structure of Aquifex aeolicus lumazine synthase by cryo-electron microscopy to 1.42 A resolution.

ABSTRACT: Single-particle cryo-electron microscopy (cryo-EM) has become an essential structural determination technique with recent hardware developments making it possible to reach atomic resolution, at which individual atoms, including hydrogen atoms, can be resolved. In this study, we used the enzyme involved in the penultimate step of riboflavin biosynthesis as a test specimen to benchmark a recently installed microscope and determine if other protein complexes could reach a resolution of 1.5 Å or better, which so far has only been achieved for the iron carrier ferritin. Using state-of-the-art microscope and detector hardware as well as the latest software techniques to overcome microscope and sample limitations, a 1.42 Å map of Aquifex aeolicus lumazine synthase (AaLS) was obtained from a 48 h

SUBMITTER: Savva CG 

PROVIDER: S-EPMC11364023 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature