https://3demmethods.i2pc.es/index.php?action=history&feed=atom&title=2024Wang_DiffModeller2024Wang DiffModeller - Revision history2026-05-24T21:06:29ZRevision history for this page on the wikiMediaWiki 1.44.2https://3demmethods.i2pc.es/index.php?title=2024Wang_DiffModeller&diff=4803&oldid=prevWikiSysop: Created page with "== Citation == X. Wang, H. Zhu, G. Terashi, M. Taluja, and D. Kihara, “DiffModeler: large macromolecular structure modeling for cryo-EM maps using a diffusion model,” Nature Methods, pp. 1–11, 2024. == Abstract == Cryogenic electron microscopy (cryo-EM) has now been widely used for determining multichain protein complexes. However, modeling a large complex structure, such as those with more than ten chains, is challenging, particularly when the map resolution de..."2024-11-08T10:16:08Z<p>Created page with "== Citation == X. Wang, H. Zhu, G. Terashi, M. Taluja, and D. Kihara, “DiffModeler: large macromolecular structure modeling for cryo-EM maps using a diffusion model,” Nature Methods, pp. 1–11, 2024. == Abstract == Cryogenic electron microscopy (cryo-EM) has now been widely used for determining multichain protein complexes. However, modeling a large complex structure, such as those with more than ten chains, is challenging, particularly when the map resolution de..."</p>
<p><b>New page</b></p><div>== Citation ==<br />
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X. Wang, H. Zhu, G. Terashi, M. Taluja, and D. Kihara, “DiffModeler: large macromolecular structure modeling for cryo-EM maps using a diffusion model,” Nature Methods, pp. 1–11, 2024.<br />
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== Abstract ==<br />
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Cryogenic electron microscopy (cryo-EM) has now been widely used for<br />
determining multichain protein complexes. However, modeling a large<br />
complex structure, such as those with more than ten chains, is challenging,<br />
particularly when the map resolution decreases. Here we present<br />
DiffModeler, a fully automated method for modeling large protein complex<br />
structures. DiffModeler employs a diffusion model for backbone tracing<br />
and integrates AlphaFold2-predicted single-chain structures for structure<br />
fitting. DiffModeler showed an average template modeling score of 0.88<br />
and 0.91 for two datasets of cryo-EM maps of 0–5 Å resolution and 0.92<br />
for intermediate resolution maps (5–10 Å), substantially outperforming<br />
existing methodologies. Further benchmarking at low resolutions (10–20 Å)<br />
confirms its versatility, demonstrating plausible performance.<br />
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== Keywords ==<br />
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== Links ==<br />
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https://www.nature.com/articles/s41592-024-02479-0<br />
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== Related software ==<br />
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== Related methods ==<br />
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== Comments ==</div>WikiSysop