Structure of catalase determined by MicroED

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

Research output: Contribution to journalArticle

39 Citations (Scopus)

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)
Pages (from-to)e03600
JournaleLife
Volume3
DOIs
StatePublished - 2014
Externally publishedYes

Fingerprint

Liver
Catalase
Electrons
Crystallography
X ray crystallography
X Ray Crystallography
Muramidase
Electron diffraction
Biological materials
Diffraction patterns
Single crystals
Crystals
Proteins

Keywords

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

ASJC Scopus subject areas

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

Cite this

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

Structure of catalase determined by MicroED. / Nannenga, Brent; Shi, Dan; Hattne, Johan; Reyes, Francis E.; Gonen, Tamir.

In: eLife, Vol. 3, 2014, p. e03600.

Research output: Contribution to journalArticle

Nannenga, B, Shi, D, Hattne, J, Reyes, FE & Gonen, T 2014, 'Structure of catalase determined by MicroED', eLife, vol. 3, pp. e03600. https://doi.org/10.7554/eLife.03600
Nannenga, Brent ; Shi, Dan ; Hattne, Johan ; Reyes, Francis E. ; Gonen, Tamir. / Structure of catalase determined by MicroED. In: eLife. 2014 ; Vol. 3. pp. e03600.
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AB - 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.

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