ArticleActa crystallographica. Section D, Biological crystallography2008
BALBES: a molecular-replacement pipeline.
Article in Acta crystallographica. Section D, Biological crystallography, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 487 papers.
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487 citing papers in PubMed.
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- Conformational flexibility associated with remote residues regulates the kinetic properties of glutamate dehydrogenase.Protein science : a publication of the Protein Society · 2025Article
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427 more citing papers are in PubMed but not listed here.
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4 authors.
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Abstract
The number of macromolecular structures solved and deposited in the Protein Data Bank (PDB) is higher than 40 000. Using this information in macromolecular crystallography (MX) should in principle increase the efficiency of MX structure solution. This paper describes a molecular-replacement pipeline, BALBES, that makes extensive use of this repository. It uses a reorganized database taken from the PDB with multimeric as well as domain organization. A system manager written in Python controls the workflow of the process. Testing the current version of the pipeline using entries from the PDB has shown that this approach has huge potential and that around 75% of structures can be solved automatically without user intervention.
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