Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB

J Biol Chem. 2021 Jan-Jun;296:100560. doi: 10.1016/j.jbc.2021.100560. Epub 2021 Mar 18.


Cryogenic electron microscopy (cryo-EM) methods began to be used in the mid-1970s to study thin and periodic arrays of proteins. Following a half-century of development in cryo-specimen preparation, instrumentation, data collection, data processing, and modeling software, cryo-EM has become a routine method for solving structures from large biological assemblies to small biomolecules at near to true atomic resolution. This review explores the critical roles played by the Protein Data Bank (PDB) and Electron Microscopy Data Bank (EMDB) in partnership with the community to develop the necessary infrastructure to archive cryo-EM maps and associated models. Public access to cryo-EM structure data has in turn facilitated better understanding of structure-function relationships and advancement of image processing and modeling tool development. The partnership between the global cryo-EM community and PDB and EMDB leadership has synergistically shaped the standards for metadata, one-stop deposition of maps and models, and validation metrics to assess the quality of cryo-EM structures. The advent of cryo-electron tomography (cryo-ET) for in situ molecular cell structures at a broad resolution range and their correlations with other imaging data introduce new data archival challenges in terms of data size and complexity in the years to come.

Keywords: cryo-electron microscopy; cryo-electron tomography; data archiving; electron crystallography; imaging; protein structure; single particle analysis.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Cryoelectron Microscopy / methods*
  • Crystallography, X-Ray
  • Databases, Protein*
  • Protein Conformation
  • Proteins / chemistry*
  • Proteins / ultrastructure


  • Proteins