| Literature DB >> 33954706 |
Abstract
Cryo-electron microscopy (cryo-EM) has become one of important experimental methods in structure determination. However, despite the rapid growth in the number of deposited cryo-EM maps motivated by advances in microscopy instruments and image processing algorithms, building accurate structure models for cryo-EM maps remains a challenge. Protein secondary structure information, which can be extracted from EM maps, is beneficial for cryo-EM structure modeling. Here, we present a novel secondary structure annotation framework for cryo-EM maps at both intermediate and high resolutions, named EMNUSS. EMNUSS adopts a three-dimensional (3D) nested U-net architecture to assign secondary structures for EM maps. Tested on three diverse datasets including simulated maps, middle resolution experimental maps, and high-resolution experimental maps, EMNUSS demonstrated its accuracy and robustness in identifying the secondary structures for cyro-EM maps of various resolutions. The EMNUSS program is freely available at http://huanglab.phys.hust.edu.cn/EMNUSS.Entities:
Keywords: EM maps; cryo-electron microscopy (cryo-EM); deep learning; nested U-net; secondary structure
Mesh:
Year: 2021 PMID: 33954706 PMCID: PMC8574626 DOI: 10.1093/bib/bbab156
Source DB: PubMed Journal: Brief Bioinform ISSN: 1467-5463 Impact factor: 11.622