The DOI matches its Crossref record; 87 of the 87 references it cites were found in a registry or an index.
Cryo-electron microscopy for structural analysis of dynamic biological macromolecules
Open accessAbstract
BACKGROUND: Since the introduction of what became today's standard for cryo-embedding of biological macromolecules at native conditions more than 30years ago, techniques and equipment have been drastically improved and the structure of biomolecules can now be studied at near atomic resolution by cryo-electron microscopy (cryo-EM) while capturing multiple dynamic states. Here we review the recent progress in cryo-EM for structural studies of dynamic biological macromolecules. SCOPE OF REVIEW: We provide an overview of the cryo-EM method and introduce contemporary studies to investigate biomolecular structure and dynamics, including examples from the recent literature. MAJOR CONCLUSIONS: Cryo-EM is a powerful tool for the investigation of biological macromolecular structures including analysis of their dynamics by using advanced image-processing algorithms. The method has become even more widely applicable with present-day single particle analysis and electron tomography. GENERAL SIGNIFICANCE: The cryo-EM method can be used to determine the three-dimensional structure of biomacromolecules in near native condition at close to atomic resolution, and has the potential to reveal conformations of dynamic molecular complexes. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.
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Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 11,626
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E., Armache, J.-P., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,777
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
Automated electron microscope tomography using robust prediction of specimen movements
Mastronarde, D. N. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,336
CTFFIND4: Fast and accurate defocus estimation from electron micrographs
Rohou, A., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.008 · Cited by 4,913
Comparative Protein Structure Modeling Using MODELLER
Webb, B., & Sali, A. (2016) · Current Protocols in Bioinformatics · doi:10.1002/cpbi.3 · Cited by 4,316
Gctf: Real-time CTF determination and correction
Zhang, K. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,537
EMAN2: An extensible image processing suite for electron microscopy
Tang, G., Peng, L., Baldwin, P. R., Mann, D. S., Jiang, W., Rees, I., & Ludtke, S. J. (2007) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.05.009 · Cited by 2,994
Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416
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Fujisaki, H., Moritsugu, K., & Matsunaga, Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103177 · Cited by 5
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Metadata
- Authors
- Murata, K., & Wolf, M.
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 2018-02
- Volume
- 1862
- Issue
- 2
- Pages
- 324-334
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W2736403501
- Cited by
- 331
- References
- 87
- FWCI
- 12.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
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