Abstract: Conventional protein:ligand crystallographic refinement uses stereochemistry restraints coupled with a rudimentary energy functional to ensure the correct geometry of the model of the macromolecule—along…
Abstract: Conventional macromolecular crystallographic refinement relies on often dubious stereochemical restraints, the preparation of which often requires human validation for unusual species, and on rudimentary…
Abstract: Gaining an understanding of the protein:ligand complex structure along with the proper protonation and explicit solvent effects can be important in obtaining meaningful results…
Abstract: There is a large body of evidence that many protein–ligand cocrystal structures contain poorly refined ligand geometries. These errors result in bound structures that…
Abstract: Macromolecular crystallographic refinement relies on sometimes dubious stereochemical restraints and rudimentary energy functionals to ensure the correct geometry of the model of the macromolecule…
Introduction In a recent paper in which we detail the treatment of 50+ structures, we demonstrate that quantum mechanics (QM)-based x-ray refinement available in Phenix/DivCon…
