ArticleJournal of structural biology2016
An approach to improve the resolution of helical filaments with a large axial rise and flexible subunits.
Article in Journal of structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- Structural basis of the super- and hyper-relaxed states of myosin II.The Journal of general physiology · 2022Review
- Article
- CryoEM structure ofLife science alliance · 2020Article
- The myosin interacting-heads motif present in live tarantula muscle explains tetanic and posttetanic phosphorylation mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Direct Visualization of Actin Filaments and Actin-Binding Proteins in Neuronal Cells.Frontiers in cell and developmental biology · 2020Review
- The central role of the tail in switching off 10S myosin II activity.The Journal of general physiology · 2019Article
- Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Biophysical reviews · 2018Review
- Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function.Biophysical reviews · 2017Review
- The Myofilament Field Revisited in the Age of Cellular and Molecular Biology.Circulation research · 2017Review
- Molecular structure of muscle filaments determined by electron microscopy.Applied microscopy · 2017Article
- Structure of myosin filaments from relaxedScience advances · 2016Article
- Conserved Intramolecular Interactions Maintain Myosin Interacting-Heads Motifs Explaining Tarantula Muscle Super-Relaxed State Structural Basis.Journal of molecular biology · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Single particle analysis is widely used for three-dimensional reconstruction of helical filaments. Near-atomic resolution has been obtained for several well-ordered filaments. However, it is still a challenge to achieve high resolution for filaments with flexible subunits and a large axial rise per subunit relative to pixel size. Here, we describe an approach that improves the resolution in such cases. In filaments with a large axial rise, many segments must be shifted a long distance along the filament axis to match with a reference projection, potentially causing loss of alignment accuracy and hence resolution. In our study of myosin filaments, we overcame this problem by pre-determining the axial positions of myosin head crowns within segments to decrease the alignment error. In addition, homogeneous, well-ordered segments were selected from the raw data set by checking the assigned azimuthal rotation angle of segments in each filament against those expected for perfect helical symmetry. These procedures improved the resolution of the filament reconstruction from 30 Å to 13 Å. This approach could be useful in other helical filaments with a large axial rise and/or flexible subunits.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.