Cited by 1,325Advanced Electron Microscopy Techniques and ApplicationsEnzyme Structure and FunctionProtein Structure and Dynamics

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The Resolution Revolution

Kühlbrandt, Werner·2014·Science

DOI 10.1126/science.1251652

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Abstract

Advances in detector technology and image processing are yielding high-resolution electron cryo-microscopy structures of biomolecules. [Also see Report by Amunts et al. ]

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Crossref · 10.1126/science.1251652

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Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327
Structure of the 30S ribosomal subunit
Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030006 · Cited by 2,035
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Schur, F. K. M., Hagen, W. J. H., de Marco, A., & Briggs, J. A. G. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.10.015 · Cited by 90

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Authors: Kühlbrandt, W.
Affiliations: Max Planck Institute of Biophysics (DE)
Corresponding author: Kühlbrandt, Werner
ORCID: Kühlbrandt, Werner
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2014-03-28
Volume: 343
Issue: 6178
Pages: 1443-1444
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1251652
OpenAlex: W2051925784
Cited by: 1,325
References: 10
Citations by year: 2026: 120 · 2025: 117 · 2024: 130 · 2023: 110 · 2022: 135 · 2021: 142 · 2020: 121 · 2019: 142 · 2018: 109 · 2017: 73 · 2016: 60 · 2015: 51 · 2014: 15
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: cryo-electron microscopy, high-resolution structure determination, biomolecular structure, detector technology, image processing
MeSH terms: Mitochondria, Saccharomyces cerevisiae, Ribosome Subunits, Large, Eukaryotic

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