The cryo-EM method microcrystal electron diffraction (MicroED)

Brent L Nannenga; Tamir Gonen

doi:10.1038/s41592-019-0395-x

The cryo-EM method microcrystal electron diffraction (MicroED)

Nat Methods. 2019 May;16(5):369-379. doi: 10.1038/s41592-019-0395-x. Epub 2019 Apr 29.

Authors

Brent L Nannenga^{1

2}, Tamir Gonen^{3

4}

Affiliations

¹ Chemical Engineering, School for Engineering of Matter, Transport, and Energy, Arizona State University, Tempe, AZ, USA. Brent.Nannenga@asu.edu.
² Center for Applied Structural Discovery, The Biodesign Institute, Arizona State University, Tempe, AZ, USA. Brent.Nannenga@asu.edu.
³ Howard Hughes Medical Institute, University of California, Los Angeles, Los Angeles, CA, USA. tgonen@g.ucla.edu.
⁴ Departments of Biological Chemistry and Physiology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA, USA. tgonen@g.ucla.edu.

Abstract

In 2013 we established a cryo-electron microscopy (cryo-EM) technique called microcrystal electron diffraction (MicroED). Since that time, data collection and analysis schemes have been fine-tuned, and structures for more than 40 different proteins, oligopeptides and organic molecules have been determined. Here we review the MicroED technique and place it in context with other structure-determination methods. We showcase example structures solved by MicroED and provide practical advice to prospective users.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

MeSH terms

Cryoelectron Microscopy / methods*
Crystallography, X-Ray / methods*
Microscopy, Electron, Transmission / methods*
Models, Molecular
Protein Conformation
Proteins / chemistry*

Substances

Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding