Structure of catalase determined by MicroED

Brent L. Nannenga, Dan Shi, Johan Hattne, Francis E. Reyes, Tamir Gonen

Research output: Contribution to journalArticle

50 Scopus citations

Abstract

MicroED is a recently developed method that uses electron diffraction for structure determination from very small three-dimensional crystals of biological material. Previously we used a series of still diffraction patterns to determine the structure of lysozyme at 2.9 Å resolution with MicroED (Shi et al., 2013). Here we present the structure of bovine liver catalase determined from a single crystal at 3.2 Å resolution by MicroED. The data were collected by continuous rotation of the sample under constant exposure and were processed and refined using standard programs for X-ray crystallography. The ability of MicroED to determine the structure of bovine liver catalase, a protein that has long resisted atomic analysis by traditional electron crystallography, demonstrates the potential of this method for structure determination.

Original languageEnglish (US)
Article numbere03600
Pages (from-to)e03600
JournaleLife
Volume3
DOIs
StatePublished - 2014

Keywords

  • MicroED
  • biochemistry
  • biophysics
  • catalase
  • cryo EM
  • electron diffraction
  • electron microscopy
  • micro crystals
  • none
  • structural biology

ASJC Scopus subject areas

  • Neuroscience(all)
  • Immunology and Microbiology(all)
  • Biochemistry, Genetics and Molecular Biology(all)

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    Nannenga, B. L., Shi, D., Hattne, J., Reyes, F. E., & Gonen, T. (2014). Structure of catalase determined by MicroED. eLife, 3, e03600. [e03600]. https://doi.org/10.7554/eLife.03600