TY - JOUR
T1 - Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB
AU - Chiu, Wah
AU - Schmid, Michael F.
AU - Pintilie, Grigore D.
AU - Lawson, Catherine L.
N1 - Publisher Copyright:
© 2021 American Society for Biochemistry and Molecular Biology Inc.. All rights reserved.
PY - 2021/1/1
Y1 - 2021/1/1
N2 - Cryogenic electronmicroscopy (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, andmodeling software, cryo-EMhas becomea routinemethod 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 ofmaps andmodels, and validationmetrics to assess the quality of cryo-EM structures. The advent of cryoelectron 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.
AB - Cryogenic electronmicroscopy (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, andmodeling software, cryo-EMhas becomea routinemethod 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 ofmaps andmodels, and validationmetrics to assess the quality of cryo-EM structures. The advent of cryoelectron 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.
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U2 - 10.1016/j.jbc.2021.100560
DO - 10.1016/j.jbc.2021.100560
M3 - Review article
C2 - 33744287
AN - SCOPUS:85104600061
SN - 0021-9258
VL - 296
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
M1 - 100560
ER -