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Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix
Abstract
Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks.
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“Model geometries were assessed using the MolProbity module in Phenix, the Molprobity server68 (http://molprobity.biochem.duke.edu/), and the PDB Validation server69 (www.wwpdb.org).”
From Structural organization of the retriever–CCC endosomal recycling complex (2024) · cites this paper as [69]
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Matplotlib: a 2D graphics environment
Hunter, J. D. (2007) · Computing in Science & Engineering · doi:10.1109/mcse.2007.55 · Cited by 39,249
PHENIX : a comprehensive Python-based system for macromolecular structure solution
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Self-citationPhaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Self-citationTowards automated crystallographic structure refinement with phenix.refine
Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., & Adams, P. D. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912001308 · Cited by 5,511
Self-citationTerwilliger, T. C., Grosse-Kunstleve, R. W., Afonine, P. V., Moriarty, N. W., Zwart, P. H., Hung, L.-W., Read, R. J., & Adams, P. D. (2008) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744490705024x · Cited by 1,462
Self-citationKühlbrandt, W. (2014) · Science · doi:10.1126/science.1251652 · Cited by 1,325
De novo modeling in cryo-EM density maps with Pathwalking
Chen, M., Baldwin, P. R., Ludtke, S. J., & Baker, M. L. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.06.004 · Cited by 82
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Metadata
- Authors
- Liebschner, D., Afonine, P. V., Baker, M. L., Bunkóczi, G., Chen, V. B., Croll, T. I., Hintze, B., Hung, L.-W., Jain, S., McCoy, A. J., Moriarty, N. W., Oeffner, R. D., Poon, B. K., Prisant, M. G., Read, R. J., Richardson, J. S., Richardson, D. C., Sammito, M. D., Sobolev, O. V., Stockwell, D. H., Terwilliger, T. C., Urzhumtsev, A. G., Videau, L. L., Williams, C. J., & Adams, P. D.
- Venue
- Acta Crystallographica Section D Structural Biology
- Published
- 2019-10-01
- Volume
- 75
- Issue
- 10
- Pages
- 861-877
- ISSN
- 2059-7983
- PMC
- PMC6778852
- Cited by
- 7,953
- References
- 7
- Licence
- Funders
- National Institutes of Health (P01GM063210, 1R01GM071939)
- US Department of Energy (DE-AC02-05CH1123.)
- Wellcome Trust (209407/Z/17/Z)
- Horizon 2020 (790122)
- French Infrastructure for Integrated Structural Biology (ANR-10-INBS-05)
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