Protein Data Bank: A Comprehensive Review of 3D Structure Holdings and Worldwide Utilization by Researchers, Educators, and Students.
Biomolecules
; 12(10)2022 10 04.
Article
en En
| MEDLINE
| ID: mdl-36291635
The Research Collaboratory for Structural Bioinformatics Protein Data Bank (RCSB PDB), funded by the United States National Science Foundation, National Institutes of Health, and Department of Energy, supports structural biologists and Protein Data Bank (PDB) data users around the world. The RCSB PDB, a founding member of the Worldwide Protein Data Bank (wwPDB) partnership, serves as the US data center for the global PDB archive housing experimentally-determined three-dimensional (3D) structure data for biological macromolecules. As the wwPDB-designated Archive Keeper, RCSB PDB is also responsible for the security of PDB data and weekly update of the archive. RCSB PDB serves tens of thousands of data depositors (using macromolecular crystallography, nuclear magnetic resonance spectroscopy, electron microscopy, and micro-electron diffraction) annually working on all permanently inhabited continents. RCSB PDB makes PDB data available from its research-focused web portal at no charge and without usage restrictions to many millions of PDB data consumers around the globe. It also provides educators, students, and the general public with an introduction to the PDB and related training materials through its outreach and education-focused web portal. This review article describes growth of the PDB, examines evolution of experimental methods for structure determination viewed through the lens of the PDB archive, and provides a detailed accounting of PDB archival holdings and their utilization by researchers, educators, and students worldwide.
Palabras clave
DNA; Open Access; Protein Data Bank; RNA; Worldwide Protein Data Bank; biological macromolecules; carbohydrates; cryogenic electron microscopy; cryogenic electron tomography; electron crystallography; macromolecular crystallography; micro-electron diffraction; nuclear magnetic resonance spectroscopy; nucleic acids; proteins; small-molecule ligands
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Biología Computacional
Límite:
Humans
Idioma:
En
Revista:
Biomolecules
Año:
2022
Tipo del documento:
Article
País de afiliación:
Estados Unidos