The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Real-time cryo-electron microscopy data preprocessing with Warp
Open accessAbstract
The acquisition of cryo-electron microscopy (cryo-EM) data from biological specimens must be tightly coupled to data preprocessing to ensure the best data quality and microscope usage. Here we describe Warp, a software that automates all preprocessing steps of cryo-EM data acquisition and enables real-time evaluation. Warp corrects micrographs for global and local motion, estimates the local defocus and monitors key parameters for each recorded micrograph or tomographic tilt series in real time. The software further includes deep-learning-based models for accurate particle picking and image denoising. The output from Warp can be fed into established programs for particle classification and 3D-map refinement. Our benchmarks show improvement in the nominal resolution, which went from 3.9 Å to 3.2 Å, of a published cryo-EM data set for influenza virus hemagglutinin. Warp is easy to install from http://github.com/cramerlab/warp and computationally inexpensive, and has an intuitive, streamlined user interface. The user-friendly software tool Warp enables automated, on-the-fly preprocessing of cryo-EM data, including motion correction, defocus estimation, particle picking and image denoising.
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Cites
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ImageNet classification with deep convolutional neural networks
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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
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Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
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Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586
A guide to machine learning for biologists
Greener, J. G., Kandathil, S. M., Moffat, L., & Jones, D. T. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00407-0 · Cited by 2,127
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885
Structural and functional analysis of a potent sarbecovirus neutralizing antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · doi:10.1101/2020.04.07.023903 · Cited by 1,752
Metadata
- Authors
- Tegunov, D., & Cramer, P.
- Venue
- Nature Methods
- Published
- 2019-10-07
- Volume
- 16
- Issue
- 11
- Pages
- 1146-1152
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W2977933365
- Cited by
- 1,332
- References
- 5
- FWCI
- 57.03
- Type
- journal article
- Language
- en
- Open access
- green
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