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.
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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.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
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
Changed by Changed by: Mgr. Eva Špillingová, učo 110713. Changed: 29/3/2017 15:05.
Abstract
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.
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