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Automating crystallographic structure solution and refinement of protein–ligand complexes

High-throughput drug-discovery and mechanistic studies often require the determination of multiple related crystal structures that only differ in the bound ligands, point mutations in the protein sequence and minor conformational changes. If performed manually, solution and refinement requires exten...

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Detalles Bibliográficos
Autores principales: Echols, Nathaniel, Moriarty, Nigel W., Klei, Herbert E., Afonine, Pavel V., Bunkóczi, Gábor, Headd, Jeffrey J., McCoy, Airlie J., Oeffner, Robert D., Read, Randy J., Terwilliger, Thomas C., Adams, Paul D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3919266/
https://www.ncbi.nlm.nih.gov/pubmed/24419387
http://dx.doi.org/10.1107/S139900471302748X
Descripción
Sumario:High-throughput drug-discovery and mechanistic studies often require the determination of multiple related crystal structures that only differ in the bound ligands, point mutations in the protein sequence and minor conformational changes. If performed manually, solution and refinement requires extensive repetition of the same tasks for each structure. To accelerate this process and minimize manual effort, a pipeline encompassing all stages of ligand building and refinement, starting from integrated and scaled diffraction intensities, has been implemented in Phenix. The resulting system is able to successfully solve and refine large collections of structures in parallel without extensive user intervention prior to the final stages of model completion and validation.