Cryo-EM targets in CASP14

Proteins. 2021 Dec;89(12):1949-1958. doi: 10.1002/prot.26216. Epub 2021 Sep 16.


Structures of seven CASP14 targets were determined using cryo-electron microscopy (cryo-EM) technique with resolution between 2.1 and 3.8 Å. We provide an evaluation of the submitted models versus the experimental data (cryo-EM density maps) and experimental reference structures built into the maps. The accuracy of models is measured in terms of coordinate-to-density and coordinate-to-coordinate fit. A-posteriori refinement of the most accurate models in their corresponding cryo-EM density resulted in structures that are close to the reference structure, including some regions with better fit to the density. Regions that were found to be less "refineable" correlate well with regions of high diversity between the CASP models and low goodness-of-fit to density in the reference structure.

Keywords: CASP; cryo-EM; electron microscopy; model evaluation; protein structure prediction.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computational Biology
  • Cryoelectron Microscopy / methods*
  • Models, Molecular*
  • Protein Conformation
  • Proteins* / chemistry
  • Proteins* / metabolism
  • Sequence Analysis, Protein
  • Software*


  • Proteins