Three-dimensional graph matching to identify secondary structure correspondence of medium-resolution cryo-em density maps

Bahareh Behkamal, Mahmoud Naghibzadeh, Mohammad Reza Saberi, Zeinab Amiri Tehranizadeh, Andrea Pagnani, Kamal Al Nasr

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Cryo-electron microscopy (cryo-EM) is a structural technique that has played a significant role in protein structure determination in recent years. Compared to the traditional methods of X-ray crystallography and NMR spectroscopy, cryo-EM is capable of producing images of much larger protein complexes. However, cryo-EM reconstructions are limited to medium-resolution (~4– 10 Å ) for some cases. At this resolution range, a cryo-EM density map can hardly be used to directly determine the structure of proteins at atomic level resolutions, or even at their amino acid residue backbones. At such a resolution, only the position and orientation of secondary structure elements (SSEs) such as α-helices and β-sheets are observable. Consequently, finding the mapping of the secondary structures of the modeled structure (SSEs-A) to the cryo-EM map (SSEs-C) is one of the primary concerns in cryo-EM modeling. To address this issue, this study proposes a novel automatic computational method to identify SSEs correspondence in three-dimensional (3D) space. Initially, through a modeling of the target sequence with the aid of extracting highly reliable features from a generated 3D model and map, the SSEs matching problem is formulated as a 3D vector matching problem. Afterward, the 3D vector matching problem is transformed into a 3D graph matching problem. Finally, a similarity-based voting algorithm combined with the principle of least conflict (PLC) concept is developed to obtain the SSEs correspondence. To evaluate the accuracy of the method, a testing set of 25 experimental and simulated maps with a maximum of 65 SSEs is selected. Comparative studies are also conducted to demonstrate the superiority of the proposed method over some state-of-the-art techniques. The results demonstrate that the method is efficient, robust, and works well in the presence of errors in the predicted secondary structures of the cryo-EM images.

Original languageEnglish (US)
Article number1773
Issue number12
StatePublished - Dec 2021
Externally publishedYes


  • 3D graph matching
  • 3D vector matching
  • Cryo-electron microscopy
  • Modeled structure
  • Protein
  • Secondary structure elements
  • Similarity-based voting algorithm

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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