Continuous mutual improvement of macromolecular structure models in the PDB and of X-ray crystallographic software: The dual role of deposited experimental data
Abstract
Accurate crystal structures of macromolecules are of high importance in the biological and biomedical fields. Models of crystal structures in the Protein Data Bank (PDB) are in general of very high quality as deposited. However, methods for obtaining the best model of a macromolecular structure from a given set of experimental X-ray data continue to progress at a rapid pace, making it possible to improve most PDB entries after their deposition by re-analyzing the original deposited data with more recent software. This possibility represents a very significant departure from the situation that prevailed when the PDB was created, when it was envisioned as a cumulative repository of static contents. A radical paradigm shift for the PDB is therefore proposed, away from the static archive model towards a much more dynamic body of continuously improving results in symbiosis with continuously improving methods and software. These simultaneous improvements in methods and final results are made possible by the current deposition of processed crystallographic data (structure-factor amplitudes) and will be supported further by the deposition of raw data (diffraction images). It is argued that it is both desirable and feasible to carry out small-scale and large-scale efforts to make this paradigm shift amore »
- Authors:
-
- Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
- Global Phasing Ltd., Cambridge (England)
- Publication Date:
- Research Org.:
- Los Alamos National Laboratory (LANL), Los Alamos, NM (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1212454
- Grant/Contract Number:
- AC52-06NA25396
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Acta Crystallographica. Section D: Biological Crystallography (Online)
- Additional Journal Information:
- Journal Name: Acta Crystallographica. Section D: Biological Crystallography (Online); Journal Volume: 70; Journal Issue: 10; Journal ID: ISSN 1399-0047
- Publisher:
- International Union of Crystallography
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 96 KNOWLEDGE MANAGEMENT AND PRESERVATION; structure determination; model quality; data analysis; software development
Citation Formats
Terwilliger, Thomas C., and Bricogne, Gerard. Continuous mutual improvement of macromolecular structure models in the PDB and of X-ray crystallographic software: The dual role of deposited experimental data. United States: N. p., 2014.
Web. doi:10.1107/S1399004714017040.
Terwilliger, Thomas C., & Bricogne, Gerard. Continuous mutual improvement of macromolecular structure models in the PDB and of X-ray crystallographic software: The dual role of deposited experimental data. United States. https://doi.org/10.1107/S1399004714017040
Terwilliger, Thomas C., and Bricogne, Gerard. Tue .
"Continuous mutual improvement of macromolecular structure models in the PDB and of X-ray crystallographic software: The dual role of deposited experimental data". United States. https://doi.org/10.1107/S1399004714017040. https://www.osti.gov/servlets/purl/1212454.
@article{osti_1212454,
title = {Continuous mutual improvement of macromolecular structure models in the PDB and of X-ray crystallographic software: The dual role of deposited experimental data},
author = {Terwilliger, Thomas C. and Bricogne, Gerard},
abstractNote = {Accurate crystal structures of macromolecules are of high importance in the biological and biomedical fields. Models of crystal structures in the Protein Data Bank (PDB) are in general of very high quality as deposited. However, methods for obtaining the best model of a macromolecular structure from a given set of experimental X-ray data continue to progress at a rapid pace, making it possible to improve most PDB entries after their deposition by re-analyzing the original deposited data with more recent software. This possibility represents a very significant departure from the situation that prevailed when the PDB was created, when it was envisioned as a cumulative repository of static contents. A radical paradigm shift for the PDB is therefore proposed, away from the static archive model towards a much more dynamic body of continuously improving results in symbiosis with continuously improving methods and software. These simultaneous improvements in methods and final results are made possible by the current deposition of processed crystallographic data (structure-factor amplitudes) and will be supported further by the deposition of raw data (diffraction images). It is argued that it is both desirable and feasible to carry out small-scale and large-scale efforts to make this paradigm shift a reality. Small-scale efforts would focus on optimizing structures that are of interest to specific investigators. Large-scale efforts would undertake a systematic re-optimization of all of the structures in the PDB, or alternatively the redetermination of groups of structures that are either related to or focused on specific questions. All of the resulting structures should be made generally available, along with the precursor entries, with various views of the structures being made available depending on the types of questions that users are interested in answering.},
doi = {10.1107/S1399004714017040},
journal = {Acta Crystallographica. Section D: Biological Crystallography (Online)},
number = 10,
volume = 70,
place = {United States},
year = {Tue Sep 30 00:00:00 EDT 2014},
month = {Tue Sep 30 00:00:00 EDT 2014}
}
Web of Science
Works referencing / citing this record:
Synchrotron Big Data Science
journal, September 2018
- Wang, Chunpeng; Steiner, Ullrich; Sepe, Alessandro
- Small, Vol. 14, Issue 46
The Integrated Resource for Reproducibility in Macromolecular Crystallography: Experiences of the first four years
journal, November 2019
- Grabowski, Marek; Cymborowski, Marcin; Porebski, Przemyslaw J.
- Structural Dynamics, Vol. 6, Issue 6
Homology-based loop modelling yields more complete crystallographic protein structures
journal, May 2018
- van Beusekom, Bart; Joosten, Krista; Hekkelman, Maarten L.
- International Union of Crystallography (IUCr)
The science is in the data
journal, October 2017
- Helliwell, John R.; McMahon, Brian; Guss, J. Mitchell
- IUCrJ, Vol. 4, Issue 6
Findable Accessible Interoperable Re-usable (FAIR) diffraction data are coming to protein crystallography
journal, April 2019
- Helliwell, John R.; Minor, Wladek; Weiss, Manfred S.
- IUCrJ, Vol. 6, Issue 3
Naked Metal Cations Swimming in Protein Crystals
journal, November 2019
- Djinović-Carugo, Kristina; Carugo, Oliviero
- Crystals, Vol. 9, Issue 11
Findable Accessible Interoperable Re-usable (FAIR) diffraction data are coming to protein crystallography
journal, April 2019
- Helliwell, John R.; Minor, Wladek; Weiss, Manfred S.
- Acta Crystallographica Section F Structural Biology Communications, Vol. 75, Issue 5
Findable Accessible Interoperable Re-usable (FAIR) diffraction data are coming to protein crystallography
journal, April 2019
- Helliwell, John R.; Minor, Wladek; Weiss, Manfred S.
- Acta Crystallographica Section D Structural Biology, Vol. 75, Issue 5