title: Accurate metal-site structures in proteins obtained by combining experimental data and quantum chemistry.
abstract: The use of molecular mechanics calculations to supplement experimental data in standard X-ray crystallography and NMR refinements is discussed and it is shown that structures can be locally improved by the use of quantum chemical calculations. Such calculations can also be used to interpret the structures, e.g. to decide the protonation state of metal-bound ligands. They have shown that metal sites in crystal structures are frequently photoreduced or disordered, which makes the interpretation of the structures hard. Similar methods can be used for EXAFS refinements to obtain a full atomic structure, rather than a set of metal-ligand distances.
authors.affiliation: Department of Theoretical Chemistry, Lund University, Chemical Centre, P. O. Box 124, SE-221 00, Lund, Sweden. Ulf.Ryde@teokem.lu.se
authors.forename: Ulf
authors.initials: U
authors.lastname: Ryde
mesh_terms: D002623:Chemistry Techniques, Analytical / Q000379:methods*; D018360:Crystallography, X-Ray; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism; D008670:Metals / Q000378:metabolism*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011789:Quantum Theory
chemical_list: D008667:Metalloproteins; D008670:Metals