WikiSysop: Created page with "== Citation == Li, T., Chen, J., Li, H., Cao, H. and Huang, S.-Y. 2025. EMProt improves structure determination from cryo-EM maps. Nature Structural & Molecular Biology. (2025), 1–10. == Abstract == Cryo-electron microscopy (cryo-EM) has become the mainstream technique for macromolecular structure determination. However, because of intrinsic resolution heterogeneity, accurate modeling of all-atom structure from cryo-EM maps remains challenging even for maps at near-..."

2025-12-30T09:25:23Z

Created page with "== Citation == Li, T., Chen, J., Li, H., Cao, H. and Huang, S.-Y. 2025. EMProt improves structure determination from cryo-EM maps. Nature Structural & Molecular Biology. (2025), 1–10. == Abstract == Cryo-electron microscopy (cryo-EM) has become the mainstream technique for macromolecular structure determination. However, because of intrinsic resolution heterogeneity, accurate modeling of all-atom structure from cryo-EM maps remains challenging even for maps at near-..."

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== Citation ==

Li, T., Chen, J., Li, H., Cao, H. and Huang, S.-Y. 2025. EMProt improves structure determination from cryo-EM maps. Nature Structural & Molecular Biology. (2025), 1–10.

== Abstract ==

Cryo-electron microscopy (cryo-EM) has become the mainstream technique
for macromolecular structure determination. However, because of intrinsic
resolution heterogeneity, accurate modeling of all-atom structure from
cryo-EM maps remains challenging even for maps at near-atomic resolution.
Addressing the challenge, we present EMProt, a fully automated method
for accurate protein structure determination from cryo-EM maps by
efficiently integrating map information and structure prediction with a
three-track attention network. EMProt is extensively evaluated on a diverse
test set of 177 experimental cryo-EM maps with up to 54 chains in a case
at <4-Å resolution, and compared to state-of-the-art methods including
DeepMainmast, ModelAngelo, phenix.dock_and_rebuild and AlphaFold3.
It is shown that EMProt greatly outperforms the existing methods in
recovering the protein structure and building the complete structure. In
addition, the built models by EMrot exhibit a high accuracy in model-to-map
fit and structure validations.

== Keywords ==

== Links ==

https://www.nature.com/articles/s41594-025-01723-1

== Related software ==

== Related methods ==

== Comments ==

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