@article {46881,
	title = {MicroED data collection and processing.},
	journal = {Acta Crystallographica Section A: Foundations \& Advances},
	volume = {71},
	year = {2015},
	month = {2015 Jul 01},
	pages = {353-60},
	abstract = {<p>MicroED, a method at the intersection of X-ray crystallography and electron cryo-microscopy, has rapidly progressed by exploiting advances in both fields and has already been successfully employed to determine the atomic structures of several proteins from sub-micron-sized, three-dimensional crystals. A major limiting factor in X-ray crystallography is the requirement for large and well ordered crystals. By permitting electron diffraction patterns to be collected from much smaller crystals, or even single well ordered domains of large crystals composed of several small mosaic blocks, MicroED has the potential to overcome the limiting size requirement and enable structural studies on difficult-to-crystallize samples. This communication details the steps for sample preparation, data collection and reduction necessary to obtain refined, high-resolution, three-dimensional models by MicroED, and presents some of its unique challenges.</p>
},
	issn = {2053-2733},
	doi = {10.1107/S2053273315010669},
	author = {Hattne, Johan and Reyes, Francis E and Nannenga, Brent L and Shi, Dan and de la Cruz, M Jason and Leslie, Andrew G W and Gonen, Tamir}
}
@article {45860,
	title = {High-resolution structure determination by continuous-rotation data collection in MicroED.},
	journal = {Nature Methods},
	volume = {11},
	year = {2014},
	month = {2014 Sep},
	pages = {927-30},
	abstract = {<p>MicroED uses very small three-dimensional protein crystals and electron diffraction for structure determination. We present an improved data collection protocol for MicroED called {\textquoteright}continuous rotation{\textquoteright}. Microcrystals are continuously rotated during data collection, yielding more accurate data. The method enables data processing with the crystallographic software tool MOSFLM, which resulted in improved resolution for the model protein lysozyme. These improvements are paving the way for the broad implementation and application of MicroED in structural biology.</p>
},
	keywords = {Algorithms, Databases, Protein, Electrons, Imaging, Three-Dimensional, Information Storage and Retrieval, Lasers, Microscopy, Video, Protein Conformation, Proteins, Rotation, Scattering, Small Angle, X-Ray Diffraction},
	issn = {1548-7105},
	doi = {10.1038/nmeth.3043},
	author = {Nannenga, Brent L and Shi, Dan and Leslie, Andrew G W and Gonen, Tamir}
}
