Structural analysis of non‐crystalline macromolecules: the ribosome

Structural analysis of non‐crystalline macromolecules: the ribosome Single‐particle analysis using cryo‐electron microscopy has emerged recently as a tool for elucidating the structure of biological macromolecules and their assemblies. A prerequisite for single‐particle analysis is an ensemble of images of structurally identical particles in different orientations. There are a variety of techniques used for image processing of this type of object in electron microscopy. The paper gives an overview of the general philosophy of image analysis of single particles in electron microscopy. It has been shown that multivariate statistical analysis of large data sets in conjunction with angular reconstitution is capable of yielding a structural resolution approaching that of X‐ray structural analysis of large macromolecules. Structure preservation during specimen preparation for electron microscopy is crucial for high‐resolution studies. Nowadays, cryo‐electron microscopy is a beneficial method for studying biological macromolecules in their natural environment, allowing their rapid freezing in a particular functional state. The processing of images of 50S Escherichia coli ribosomal subunits embedded in vitreous ice is used as an example of image analysis of single particles at 7.5 Å resolution. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section D Wiley

Structural analysis of non‐crystalline macromolecules: the ribosome

Acta Crystallographica Section D, Volume 56 (10) – Oct 1, 2000

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Publisher
Wiley
Copyright
Copyright © 2000 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1399-0047
eISSN
1399-0047
DOI
10.1107/S090744490001115X
Publisher site
See Article on Publisher Site

Abstract

Single‐particle analysis using cryo‐electron microscopy has emerged recently as a tool for elucidating the structure of biological macromolecules and their assemblies. A prerequisite for single‐particle analysis is an ensemble of images of structurally identical particles in different orientations. There are a variety of techniques used for image processing of this type of object in electron microscopy. The paper gives an overview of the general philosophy of image analysis of single particles in electron microscopy. It has been shown that multivariate statistical analysis of large data sets in conjunction with angular reconstitution is capable of yielding a structural resolution approaching that of X‐ray structural analysis of large macromolecules. Structure preservation during specimen preparation for electron microscopy is crucial for high‐resolution studies. Nowadays, cryo‐electron microscopy is a beneficial method for studying biological macromolecules in their natural environment, allowing their rapid freezing in a particular functional state. The processing of images of 50S Escherichia coli ribosomal subunits embedded in vitreous ice is used as an example of image analysis of single particles at 7.5 Å resolution.

Journal

Acta Crystallographica Section DWiley

Published: Oct 1, 2000

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