Published September 30, 2010 | Version public
Book Section - Chapter

Preface

Contributors

Abstract

In this, the fifty-fourth year of Methods in Enzymology, we celebrate the discovery and initial characterization of thousands of individual enzymes, the sequencing of hundreds of whole genomes, and the structure determination of tens of thousands of proteins. In this context, the architectures of multienyzme/multiprotein complexes and their arrangement within cells have now come to the fore. A uniquely powerful method in this field is electron cryomicroscopy (cryo-EM), which in its broadest sense, is all those techniques that image cold samples in the electron microscope. Cryo-EM allows individual enzymes and proteins, macromolecular complexes, assemblies, cells, and even tissues to be observed in a "frozen-hydrated," near-native state free from the artifacts of fixation, dehydration, plastic-embedding, or staining typically used in traditional forms of EM (Chapter 3, Vol. 481). This series of volumes is therefore dedicated to a description of the instruments, samples, protocols, and analyses that belong to the growing field of cryo-EM.

Additional Information

© 2010 Elsevier Inc. Available online 30 September 2010.

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Identifiers

Eprint ID
103076
DOI
10.1016/s0076-6879(10)83021-6
Resolver ID
CaltechAUTHORS:20200507-132959366

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Dates

Created
2020-05-07
Created from EPrint's datestamp field
Updated
2021-11-16
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Series Name
Methods in Enzymology
Series Volume or Issue Number
483