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MicroED opens a new era for biological structure determination.

Brent L Nannenga1, Tamir Gonen2

  • 1Chemical Engineering, School for Engineering of Matter, Transport, and Energy, Arizona State University, Tempe, AZ 85287, USA.

Current Opinion in Structural Biology
|October 5, 2016
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Summary
This summary is machine-generated.

Microcrystal electron diffraction (MicroED) uses cryogenic electron microscopy to determine atomic-resolution structures from tiny crystals. This review overviews MicroED and compares it to other cryo-electron microscopy techniques.

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Area of Science:

  • Structural biology
  • Biophysics
  • Crystallography

Background:

  • Cryo-electron microscopy (CryoEM) has revolutionized structural determination.
  • Microcrystal electron diffraction (MicroED) emerged in 2013 as a novel CryoEM technique.
  • MicroED enables atomic resolution structure determination from microscopic crystals.

Purpose of the Study:

  • To provide an overview of the MicroED method.
  • To compare MicroED with other CryoEM techniques.
  • To highlight the capabilities of MicroED in structural biology.

Main Methods:

  • MicroED utilizes microscopic crystals of biological material.
  • Data collection is performed in an electron microscope under cryogenic conditions.
  • Standard X-ray crystallography software is employed for data processing.

Main Results:

  • MicroED allows for the determination of structures at atomic resolution.
  • The method is effective for samples that form only tiny crystals.
  • Comparison with other CryoEM methods is discussed.

Conclusions:

  • MicroED is a powerful technique for high-resolution structure determination.
  • It complements existing CryoEM methods, expanding structural biology's reach.
  • Further development and application of MicroED are anticipated.