The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Ultrastable gold substrates for electron cryomicroscopy
Open accessAbstract
Despite recent advances, the structures of many proteins cannot be determined by electron cryomicroscopy because the individual proteins move during irradiation. This blurs the images so that they cannot be aligned with each other to calculate a three-dimensional density. Much of this movement stems from instabilities in the carbon substrates used to support frozen samples in the microscope. Here we demonstrate a gold specimen support that nearly eliminates substrate motion during irradiation. This increases the subnanometer image contrast such that α helices of individual proteins are resolved. With this improvement, we determine the structure of apoferritin, a smooth octahedral shell of α-helical subunits that is particularly difficult to solve by electron microscopy. This advance in substrate design will enable the solution of currently intractable protein structures.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638
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
Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416
Cited by
EMRinger: side chain–directed model and map validation for 3D cryo-electron microscopy
Barad, B. A., Echols, N., Wang, R. Y.-R., Cheng, Y., DiMaio, F., Adams, P. D., & Fraser, J. S. (2015) · Nature Methods · doi:10.1038/nmeth.3541 · Cited by 886
Structure of mycobacterial ATP synthase bound to the tuberculosis drug bedaquiline
Guo, H., Courbon, G. M., Bueler, S. A., Mai, J., Liu, J., & Rubinstein, J. L. (2021) · Nature · doi:10.1038/s41586-020-3004-3 · Cited by 200
Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold
Fontana, P., Dong, Y., Pi, X., Tong, A. B., Hecksel, C. W., Wang, L., Fu, T.-M., Bustamante, C., & Wu, H. (2022) · Science · doi:10.1126/science.abm9326 · Cited by 195
Structure of the STRA6 receptor for retinol uptake
Chen, Y., Clarke, O. B., Kim, J., Stowe, S., Kim, Y.-K., Assur, Z., Cavalier, M., Godoy-Ruiz, R., von Alpen, D. C., Manzini, C., et al. (2016) · Science · doi:10.1126/science.aad8266 · Cited by 148
Mechanisms of Channel Block in Calcium-Permeable AMPA Receptors
Twomey, E. C., Yelshanskaya, M. V., Vassilevski, A. A., & Sobolevsky, A. I. (2018) · Neuron · doi:10.1016/j.neuron.2018.07.027 · Cited by 106
Rieske head domain dynamics and indazole-derivative inhibition of Candida albicans complex III
Di Trani, J. M., Liu, Z., Whitesell, L., Brzezinski, P., Cowen, L. E., & Rubinstein, J. L. (2022) · Structure · doi:10.1016/j.str.2021.08.006 · Cited by 32
Structure and design of Langya virus glycoprotein antigens
Wang, Z., McCallum, M., Yan, L., Gibson, C. A., Sharkey, W., Park, Y.-J., Dang, H. V., Amaya, M., Person, A., Broder, C. C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2314990121 · Cited by 32
Structural basis of V-ATPase V O region assembly by Vma12p, 21p, and 22p
Wang, H., Bueler, S. A., & Rubinstein, J. L. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217181120 · Cited by 18
Cryo‐EM structures of multiple‐peptide resistance factor ( MprF ) from Pseudomonas aeruginosa
Jha, S., & Vinothkumar, K. R. (2026) · The FEBS Journal · doi:10.1111/febs.70519 · Cited by 1
Metadata
- Authors
- Russo, C. J., & Passmore, L. A.
- Venue
- Science
- Published
- 2014-12-12
- Volume
- 346
- Issue
- 6215
- Pages
- 1377-1380
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1967004359
- Cited by
- 400
- References
- 3
- FWCI
- 12.05
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
