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 language | English (US) |
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Article number | e03600 |
Pages (from-to) | e03600 |
Journal | eLife |
Volume | 3 |
DOIs | |
State | Published - 2014 |
Externally published | Yes |
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)