Automating crystallographic structure solution and refinement of protein-ligand complexes

A software system for automated protein-ligand crystallography has been implemented in the Phenix suite. This significantly reduces the manual effort required in high-throughput crystallographic studies.

Automated identification of elemental ions in macromolecular crystal structures

The solvent-picking procedure in phenix.refine has been extended and combined with Phaser anomalous substructure completion and analysis of coordination geometry to identify and place elemental ions.

Flexible torsion-angle noncrystallographic symmetry restraints for improved macromolecular structure refinement

Flexible torsion angle-based NCS restraints have been implemented in phenix.refine, allowing improved model refinement at all resolutions. Rotamer correction and rotamer consistency checks between NCS-related amino-acid side chains further improve the final model quality.

Metrics for comparison of crystallographic maps

Rank scaling of Fourier syntheses leads to new tools for the comparison of crystallographic contour maps. The new metrics are in better agreement with a visual map analysis than the conventional map correlation coefficient.