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ZENODO
Journal . 2010
License: CC BY
Data sources: ZENODO
ZENODO
Journal . 2010
License: CC BY
Data sources: Datacite
ZENODO
Journal . 2010
License: CC BY
Data sources: Datacite
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A Redesigned Database of Three-dimensional Protein Structures for Reuse in Macromolecular Crystallography

descriptionPublicationkeyboard_double_arrow_right Journal 13 Oct 2010 English Publisher:Zenodo
Authors: Alexei A. Vagin; Fei Long; Garib N. Murshudov;

doi: 10.5281/zenodo.10023879 , 10.5281/zenodo.10023878

A Redesigned Database of Three-dimensional Protein Structures for Reuse in Macromolecular Crystallography

Abstract

The number of macromolecular structures solved and deposited to the Protein Data Bank (PDB) ismore than 66000. Exploiting this information for macromolecular crystallography (MX) dramaticallyincreases the efficiency of MX structure solution. This paper describes a database of "unique" PDBentries with their domains and potential oligemeric states. The database is used, as a proof of prin-ciple, in one of the automatic MX structure solution pipelines. Tests with the new entries from the PDBshows that the pipeline based on this database is able to solve around 80% of all solvable structuresautomatically.

Keywords

macromolecular crystallography, protein structures, database, domains

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
0
Average
Average
Average
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