Single-particle cryo-EM of biological macromolecules /

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"Version: 20210205"--Title page verso.Includes bibliographical references.1. Introduction and overview -- 1.1. Visualizing biological molecules to understand life's principles -- 1.2. Recovery of 3D structures from images of weak-phase objects2. Sample preparation -- 2.1. Overview -- 2.2. Initial screening of samples in negative stain -- 2.3. Standard method of making grids for cryo-EM -- 2.4. Requirement to make very thin specimens for cryo-EM -- 2.5. Current strategies for optimizing preparation of cryo-grids3. Data collection -- 3.1. Overview -- 3.2. Radiation damage in cryo-EM -- 3.3. Low-dose protocols for recording images -- 3.4. Practical considerations : defocus, stigmation, coma-free illumination, and phase plates -- 3.5. Practical considerations : movie-mode data acquisition4. Data processing -- 4.1. Overview -- 4.2. Automated extraction of particles -- 4.3. CTF estimation and image correction (restoration) -- 4.4. Merging data from structurally homogeneous subsets -- 4.5. 3D classification of structurally heterogeneous particles -- 4.6. Preferred orientation : how to recognize and deal with adverse effects -- 4.7. B factors and map sharpening -- 4.8. Optical aberrations and Ewald sphere curvature5. Map validation -- 5.1. Overview -- 5.2. Measures of resolution : FSC and local resolution -- 5.3. Recognizing the effect of bias and over-fitting -- 5.4. Estimates of alignment accuracy -- 5.5. Discussion6. Model building and validation -- 6.1. Overview -- 6.2. Using known components or homologs : model building -- 6.3. Building atomistic models in cryo-EM density maps -- 6.4. Quality evaluation of cryo-EM map-derived models -- 6.5. How algorithms from crystallography are helping electron cryo-microscopy -- 6.6. Archiving structures and data.This edited book is written for students, postdocs and established investigators who want to enter the field of single-particle cryo-EM. This is a recently developed method to determine high-resolution structures of biological macromolecules. A major strength is the fact that cryo-EM does not require prior crystallization of protein complexes. It is especially well suited for larger complexes and molecular machines. This book provides a comprehensive, accessible and authoritative introduction to the field. It covers all necessary background, ranging from the underlying concepts to practical aspects such as specimen preparation, data collection, data analysis, and the final validation of results.Beginning scientists in academia, pharma, and biotech.Also available in print.Mode of access: World Wide Web.System requirements: Adobe Acrobat Reader, EPUB reader, or Kindle reader.Professor Glaeser (UC Berkeley) made major contributions to the initial development of cryo-EM technology, and he currently is active in the improvement of specimen preparation. Professor Nogales (UC Berkeley) has used cryo-EM throughout her scientific career, successfully applying this technique for the last three decades to systems that defied structural characterization. Professor Chiu (Stanford University) developed early experimental and computational methods toward 3D structure determination of biomolecules toward atomic resolution.Title from PDF title page (viewed on June 11, 2021).

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Call Number

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Publisher

: .,

Collation

1 online resource (various pagings) :illustrations (some color).

Language

English

ISBN/ISSN

9780750330398

Classification

574.19/283

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Media Type

-

Carrier Type

-

Edition

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Subject(s)

Biophysics.
SCIENCE / Life Sciences / Biophysics.
Macromolecules
Biomolecules
High resolution imaging.

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Statement of Responsibility

edited by Robert M. Glaeser, Eva Nogales, Wah Chiu.

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