Deciphering Protein Secondary Structures and Nucleic Acids in Cryo-EM Maps Using Deep Learning

With the resolution revolution of cryo-electron microscopy (cryo-EM) and the rapid development of image processing technology, cryo-EM has become an indispensable experimental method for determining the three-dimensional structures of biological macromolecules. However, structural modeling from cryo-EM maps remains a difficult task for intermediate-resolution maps. In such cases, detection of protein secondary structures and nucleic acid locations in an EM map is of great value for model building of the map. Meeting the need, we present a deep learning-based method for detecting protein secondary structures and nucleic acid locations in cryo-EM density maps, named EMInfo. EMInfo was extensively evaluated on two protein-nucleic acid complex test sets including intermediate-resolution experimental maps and high-resolution experimental maps and compared them with two state-of-the-art methods including Emap2sec+ and Haruspex. It is shown that EMInfo can accurately predict different structural categories in an EM map. EMInfo is freely available at http://huanglab.phys.hust.edu.cn/EMInfo/.

Authors

Institutions

Publication Details

Journal
Journal of Chemical Information and Modeling
Published
2025-01-22
DOI
https://doi.org/10.1021/acs.jcim.4c01971
Citations
3
Primary Topic
Advanced Electron Microscopy Techniques and Applications
Type
article
Field-Weighted Citation Impact
7.65

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Deciphering Protein Secondary Structures and Nucleic Acids in Cryo-EM Maps Using Deep Learning

Hong Cao, Sheng‐You Huang, Jiahua He, Tao Li
3 citations
Journal of Chemical Information and Modeling
Advanced Electron Microscopy Techniques and Applications
7.65
article

Deciphering Protein Secondary Structures and Nucleic Acids in Cryo-EM Maps Using Deep Learning

Hong Cao, Sheng‐You Huang, Jiahua He, Tao Li
article en
3 citations

Abstract

With the resolution revolution of cryo-electron microscopy (cryo-EM) and the rapid development of image processing technology, cryo-EM has become an indispensable experimental method for determining the three-dimensional structures of biological macromolecules. However, structural modeling from cryo-EM maps remains a difficult task for intermediate-resolution maps. In such cases, detection of protein secondary structures and nucleic acid locations in an EM map is of great value for model building of the map. Meeting the need, we present a deep learning-based method for detecting protein secondary structures and nucleic acid locations in cryo-EM density maps, named EMInfo. EMInfo was extensively evaluated on two protein-nucleic acid complex test sets including intermediate-resolution experimental maps and high-resolution experimental maps and compared them with two state-of-the-art methods including Emap2sec+ and Haruspex. It is shown that EMInfo can accurately predict different structural categories in an EM map. EMInfo is freely available at http://huanglab.phys.hust.edu.cn/EMInfo/.

Journal of Chemical Information and ModelingVol. 65(3)
Huazhong University of Science and Technology (CN)
National Natural Science Foundation of China, Huazhong University of Science and Technology
Zero hunger
Openalex Percentile: Top 5%
Advanced Electron Microscopy Techniques and Applications
7.65
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

Deciphering Protein Secondary Structures and Nucleic Acids in Cryo-EM Maps Using Deep Learning — Hong Cao, Sheng‐You Huang, et al. · Journal of Chemical Information and Modeling (2025) | TGRS Research Map | TGRS