Improved low-resolution crystallographic refinement with Phenix and Rosetta
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Updated: May 7, 2026

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
Published on: December 1, 2020
Frank DiMaio1, Nathaniel Echols, Jeffrey J Headd
11] Department of Biochemistry, University of Washington, Seattle, Washington, USA. [2].
Abstract:
Refinement of macromolecular structures against low-resolution crystallographic data is limited by the ability of current methods to converge on a structure with realistic geometry. We developed a low-resolution crystallographic refinement method that combines the Rosetta sampling methodology and energy function with reciprocal-space X-ray refinement in Phenix. On a set of difficult low-resolution cases, the method yielded improved model geometry and lower free R factors than alternate refinement methods.

