A new default restraint library for the protein backbone in Phenix: a conformation-dependent geometry goes mainstream

By Nigel W. Moriarty, D. Tronrud, Paul D. Adams, Paul Karplus. 2016

31 citations recorded by the source corpus.

The default geometry restraints used in Phenix for the protein backbone have been upgraded to account for the known conformation-dependencies of bond angles and lengths.

Subfields: Materials Chemistry, Molecular Biology

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In Materials Chemistry

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Citations in the corpus

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix (2019, methodology): “Recent additions to the restraints used in Phenix include the conformation-dependent library (Berkholz et al., 2009; Moriarty et al., 2014, 2016), which restrains the protein main chain as a function of the backbone dihedral values.”
An editor for the generation and customization of geometry restraints (2017, background): “…are becoming standard practice in structure refinement: single-value restraints have been shown to be inadequate for the protein backbone, and the Conformation Dependent Library (CDL; Berkholz et al., 2009) has recently been made the default in phenix.refine (Moriarty et al., 2014, 2016).”