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MicroED opens a new era for biological structure determination.

ABSTRACT: In 2013 we unveiled the cryo-electron microscopy (CryoEM) method of MicroED, or three-dimensional (3D) electron diffraction of microscopic crystals. Here tiny 3D crystals of biological material are used in an electron microscope for diffraction data collection under cryogenic conditions. The data is indexed, integrated, merged and scaled using standard X-ray crystallography software to determine structures at atomic resolution. In this review we provide an overview of the MicroED method and compare it with other CryoEM methods.

SUBMITTER: Nannenga BL

PROVIDER: S-EPMC5656569 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

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MicroED opens a new era for biological structure determination.

Nannenga Brent L BL Gonen Tamir T

Current opinion in structural biology 20161001

In 2013 we unveiled the cryo-electron microscopy (CryoEM) method of MicroED, or three-dimensional (3D) electron diffraction of microscopic crystals. Here tiny 3D crystals of biological material are used in an electron microscope for diffraction data collection under cryogenic conditions. The data is indexed, integrated, merged and scaled using standard X-ray crystallography software to determine structures at atomic resolution. In this review we provide an overview of the MicroED method and comp ...[more]

PMID: 27701014

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Beyond protein structure determination with MicroED.

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Polymorphic Structure Determination of the Macrocyclic Drug Paritaprevir by MicroED.

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Structure Determination from Lipidic Cubic Phase Embedded Microcrystals by MicroED.

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The CryoEM Method MicroED as a Powerful Tool for Small Molecule Structure Determination.

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Fragment-based determination of a proteinase K structure from MicroED data using ARCIMBOLDO_SHREDDER.

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The complementarity of serial femtosecond crystallography and MicroED for structure determination from microcrystals.

Project description:In recent years, nano and microcrystals have emerged as a valuable source of high-resolution structural information owing to the invention of serial femtosecond crystallography (SFX) with X-ray free electron lasers and microcrystal electron diffraction (MicroED) using electron cryomicroscopes. Once considered useless for structure determination, nano/microcrystals now confer significant advantages for static and time-resolved structure determination from a wide variety of difficult-to-study targets. MicroED has been used to obtain sub-Ångstrom resolution maps in which hydrogen atoms can be clearly resolved from only a few nano/microcrystals, while SFX has been used to probe protein dynamics following reaction initiation on time scales from femtoseconds to minutes. We review these two complementary techniques and their abilities for high-resolution structure determination.

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