Malaspina, Lorraine A.Wieduwilt, Erna K.Bergmann, JustinKleemiss, FlorianMeyer, BenjaminRuiz-Lopez, Manuel F.Pal, RumpaHupf, EmanuelBeckmann, JensPiltz, Ross O.Edwards, Alison J.Grabowsky, SimonGenoni, Alessandro2019-12-042019-12-042019-12-042019-11-2110.1021/acs.jpclett.9b02646https://infoscience.epfl.ch/handle/20.500.14299/163544WOS:000497261200002The coupling of the crystallographic refinement technique Hirshfeld atom refinement (HAR) with the recently constructed libraries of extremely localized molecular orbitals (ELMOs) gives rise to the new quantum-crystallographic method HAR-ELMO. This method is significantly faster than HAR but as accurate and precise, especially concerning the free refinement of hydrogen atoms from X-ray diffraction data, so that the first fully quantum-crystallographic refinement of a protein is presented here. However, the promise of HAR-ELMO exceeds large molecules and protein crystallography. In fact, it also renders possible electron-density investigations of heavy elements in small molecules and facilitates the detection and isolation of systematic errors from physical effects.Chemistry, PhysicalNanoscience & NanotechnologyMaterials Science, MultidisciplinaryPhysics, Atomic, Molecular & ChemicalChemistryScience & Technology - Other TopicsMaterials SciencePhysicsprotein crystallographyelectron-distributionmolecular-structurecrystal-structurescharge-densitieshigh-resolutionbond lengthsdata-bankl-alaninerefinementtext::journal::journal article::research article