@article {45552,
	title = {Structure of catalase determined by MicroED.},
	journal = {eLife},
	volume = {3},
	year = {2014},
	month = {2014 Oct 17},
	pages = {e03600},
	abstract = {<p>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 {\r A} resolution with MicroED (Shi et al., 2013). Here we present the structure of bovine liver catalase determined from a single crystal at 3.2 {\r A} 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.</p>
},
	issn = {2050-084X},
	doi = {10.7554/eLife.03600},
	author = {Nannenga, Brent L and Shi, Dan and Hattne, Johan and Reyes, Francis E and Gonen, Tamir}
}
