title: Studying protein-ligand interactions using X-ray crystallography.
abstract: X-ray crystallography is a powerful technique for studying protein-ligand interactions. Advances in techniques have meant that it is now possible to routinely determine the structures of ligand complexes in the majority of cases where crystallization conditions and protein structures are already known. Ligand soaking or cocrystallization, together with the potential use of molecular replacement, provides data for determining the structures of a protein in complex with ligands. Furthermore, advances in protein structure model building facilitate automatic ligand fitting to residual electron density in the protein-ligand complex.
authors.affiliation: CRT Discovery Laboratories, Department of Biological Sciences, Birkbeck, University of London, London, UK.
authors.forename: Andrew P
authors.initials: AP
authors.lastname: Turnbull
authors.forename: Paul
authors.initials: P
authors.lastname: Emsley
mesh_terms: D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D066246:ErbB Receptors / Q000737:chemistry*; D000077156:Gefitinib; D006801:Humans; D007700:Kinetics; D008024:Ligands; D062105:Molecular Docking Simulation; D009363:Neoplasm Proteins / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011799:Quinazolines / Q000737:chemistry*; D012984:Software; D013629:Tamoxifen / Q000031:analogs & derivatives* / Q000737:chemistry
chemical_list: D008024:Ligands; D009363:Neoplasm Proteins; D011799:Quinazolines; C038865:estrogen regulated protein; D013629:Tamoxifen; C016601:afimoxifene; C512478:EGFR protein, human; D066246:ErbB Receptors; D000077156:Gefitinib