title: Crystallographic refinement of ligand complexes.
abstract: Model building and refinement of complexes between biomacromolecules and small molecules requires sensible starting coordinates as well as the specification of restraint sets for all but the most common non-macromolecular entities. Here, it is described why this is necessary, how it can be accomplished and what pitfalls need to be avoided in order to produce chemically plausible models of the low-molecular-weight entities. A number of programs, servers, databases and other resources that can be of assistance in the process are also discussed.
authors.affiliation: Department of Cell and Molecular Biology, Uppsala University, Biomedical Centre, Box 596, SE-751 24 Uppsala, Sweden.
authors.forename: Gerard J
authors.initials: GJ
authors.lastname: Kleywegt
mesh_terms: D000818:Animals; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D030562:Databases, Protein; D004583:Electrons; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D046911:Macromolecular Substances; D008956:Models, Chemical; D008958:Models, Molecular; D015233:Models, Statistical; D008968:Molecular Conformation; D008970:Molecular Weight; D011506:Proteins / Q000737:chemistry*
chemical_list: D008024:Ligands; D046911:Macromolecular Substances; D011506:Proteins