FUTURE PROSPECTS

ROSSMANN, Michael G., Anthony J. BATTISTI and Pavel PLEVKA. FUTURE PROSPECTS. ADVANCES IN PROTEIN CHEMISTRY AND STRUCTURAL BIOLOGY, VOL 82: RECENT ADVANCES IN ELECTRON CRYOMICROSCOPY, PT B. SAN DIEGO: ELSEVIER ACADEMIC PRESS INC, 2011, vol. 82, neuvedeno, p. 101-121. ISSN 1876-1623. Available from: https://dx.doi.org/10.1016/B978-0-12-386507-6.00005-1.

Basic information

Original name

FUTURE PROSPECTS

Authors

ROSSMANN, Michael G., Anthony J. BATTISTI and Pavel PLEVKA

Edition

ADVANCES IN PROTEIN CHEMISTRY AND STRUCTURAL BIOLOGY, VOL 82: RECENT ADVANCES IN ELECTRON CRYOMICROSCOPY, PT B, SAN DIEGO, ELSEVIER ACADEMIC PRESS INC, 2011, 1876-1623

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Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 1.833

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1016/B978-0-12-386507-6.00005-1

UT WoS

000290775200005

Keywords in English

3-DIMENSIONAL FOURIER SYNTHESIS; X-RAY ANALYSIS; CRYOELECTRON TOMOGRAPHY; ELECTRON-MICROSCOPY; ATOMIC MODELS; NEUTRALIZING ANTIBODY; INTERATOMIC DISTANCES; MOLECULAR-STRUCTURE; CRYSTAL-STRUCTURES; CANINE PARVOVIRUS

Tags

neMU

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Abstract

V originále

Cryo-electron microscopy (cryo-EM) in combination with single-particle analysis has begun to complement crystallography in the study of large macromolecules at near-atomic resolution. Furthermore, advances in cryo-electron tomography have made possible the study of macromolecules within their cellular environment. Single-particle and tomographic studies will become even more useful when technologies for improving the signal-to-noise ratio such as direct electron detectors and phase plates become widely available. Automated image acquisition has significantly reduced the time and effort required to determine the structures of macromolecular assemblies. As a result, the number of structures determined by cryo-EM is growing exponentially. However, there is an urgent need for improved criteria for validating both the reconstruction process and the atomic models derived from cryo-EM data. Another major challenge will be mitigating the effects of anisotropy caused by the missing wedge and the excessively low signal-to-noise ratio for tomographic data. Parallels between the development of macromolecular crystallography and cryo-EM have been used to tentatively predict the future of cryo-EM.