{
  "id": 566556,
  "title": "Bacterial Flagellar Motor: PyMol and ChimeraX visualization programs for Biocomputing.",
  "url": "/competitions/byu-locating-bacterial-flagellar-motors-2025/discussion/566556",
  "author_name": "Marília Prata",
  "post_date": "2025-03-06T02:35:09.478000",
  "votes": 18,
  "comment_count": 0,
  "views": 0,
  "content": "<h3>Bacterial Flagellar Motor</h3>\n<p>Citation: Tan, J., Zhang, L., Zhou, X. et al. Structural basis of the bacterial flagellar motor rotational switching. Cell Res 34, 788–801 (2024). <a href=\"https://doi.org/10.1038/s41422-024-01017-z\" target=\"_blank\">https://doi.org/10.1038/s41422-024-01017-z</a></p>\n<p>Structural basis of the bacterial flagellar motor rotational switching</p>\n<p>\"The bacterial flagellar motor is a huge bidirectional rotary nanomachine that drives rotation of the flagellum for bacterial motility. The cytoplasmic C ring of the flagellar motor functions as the switch complex for the rotational direction switching from counterclockwise to clockwise. However, the structural basis of the rotational switching and how the C ring is assembled have long remained elusive.\"</p>\n<p>\"That study provides unprecedented molecular insights into the rotational switching mechanism and a detailed overall structural view of the bacterial flagellar motors.\"</p>\n<p>\"All final models were validated using MolProbity.56 Root mean square deviation (RMSD) values and the electrostatic distributions were calculated using <strong>PyMol</strong>. The model resolutions were estimated by phenix.mtriage using the model-based noise-free and experimental maps with an FSC criterion of 0.5. Angle and distance measurements were performed in <strong>ChimeraX.</strong>\"</p>\n<p><a href=\"https://www.nature.com/articles/s41422-024-01017-z#Bib1\" target=\"_blank\">https://www.nature.com/articles/s41422-024-01017-z#Bib1</a></p>",
  "messages": [
    {
      "id": 3141981,
      "postDate": "2025-03-06T02:35:09.477Z",
      "content": "<h3>Bacterial Flagellar Motor</h3>\n<p>Citation: Tan, J., Zhang, L., Zhou, X. et al. Structural basis of the bacterial flagellar motor rotational switching. Cell Res 34, 788–801 (2024). <a href=\"https://doi.org/10.1038/s41422-024-01017-z\" target=\"_blank\">https://doi.org/10.1038/s41422-024-01017-z</a></p>\n<p>Structural basis of the bacterial flagellar motor rotational switching</p>\n<p>\"The bacterial flagellar motor is a huge bidirectional rotary nanomachine that drives rotation of the flagellum for bacterial motility. The cytoplasmic C ring of the flagellar motor functions as the switch complex for the rotational direction switching from counterclockwise to clockwise. However, the structural basis of the rotational switching and how the C ring is assembled have long remained elusive.\"</p>\n<p>\"That study provides unprecedented molecular insights into the rotational switching mechanism and a detailed overall structural view of the bacterial flagellar motors.\"</p>\n<p>\"All final models were validated using MolProbity.56 Root mean square deviation (RMSD) values and the electrostatic distributions were calculated using <strong>PyMol</strong>. The model resolutions were estimated by phenix.mtriage using the model-based noise-free and experimental maps with an FSC criterion of 0.5. Angle and distance measurements were performed in <strong>ChimeraX.</strong>\"</p>\n<p><a href=\"https://www.nature.com/articles/s41422-024-01017-z#Bib1\" target=\"_blank\">https://www.nature.com/articles/s41422-024-01017-z#Bib1</a></p>",
      "rawMarkdown": "### Bacterial Flagellar Motor\n\nCitation: Tan, J., Zhang, L., Zhou, X. et al. Structural basis of the bacterial flagellar motor rotational switching. Cell Res 34, 788–801 (2024). https://doi.org/10.1038/s41422-024-01017-z\n\nStructural basis of the bacterial flagellar motor rotational switching\n\n\"The bacterial flagellar motor is a huge bidirectional rotary nanomachine that drives rotation of the flagellum for bacterial motility. The cytoplasmic C ring of the flagellar motor functions as the switch complex for the rotational direction switching from counterclockwise to clockwise. However, the structural basis of the rotational switching and how the C ring is assembled have long remained elusive.\"\n\n\"That study provides unprecedented molecular insights into the rotational switching mechanism and a detailed overall structural view of the bacterial flagellar motors.\"\n\n\"All final models were validated using MolProbity.56 Root mean square deviation (RMSD) values and the electrostatic distributions were calculated using **PyMol**. The model resolutions were estimated by phenix.mtriage using the model-based noise-free and experimental maps with an FSC criterion of 0.5. Angle and distance measurements were performed in **ChimeraX.**\"\n\nhttps://www.nature.com/articles/s41422-024-01017-z#Bib1",
      "votes": 18
    }
  ],
  "comments": [],
  "raw_markdown_by_id": {
    "3141981": "### Bacterial Flagellar Motor\n\nCitation: Tan, J., Zhang, L., Zhou, X. et al. Structural basis of the bacterial flagellar motor rotational switching. Cell Res 34, 788–801 (2024). https://doi.org/10.1038/s41422-024-01017-z\n\nStructural basis of the bacterial flagellar motor rotational switching\n\n\"The bacterial flagellar motor is a huge bidirectional rotary nanomachine that drives rotation of the flagellum for bacterial motility. The cytoplasmic C ring of the flagellar motor functions as the switch complex for the rotational direction switching from counterclockwise to clockwise. However, the structural basis of the rotational switching and how the C ring is assembled have long remained elusive.\"\n\n\"That study provides unprecedented molecular insights into the rotational switching mechanism and a detailed overall structural view of the bacterial flagellar motors.\"\n\n\"All final models were validated using MolProbity.56 Root mean square deviation (RMSD) values and the electrostatic distributions were calculated using **PyMol**. The model resolutions were estimated by phenix.mtriage using the model-based noise-free and experimental maps with an FSC criterion of 0.5. Angle and distance measurements were performed in **ChimeraX.**\"\n\nhttps://www.nature.com/articles/s41422-024-01017-z#Bib1"
  }
}