X-ray crystallography is considered the most powerful method for determining 3D structures of biological macromolecules — such as proteins and nucleic acids — and their complexes with other macromolecules or ligands, substrates and inhibitors. It is the fastest, least expensive and most successful method in structural biology — no single experimental technique produces more-detailed data about a macromolecule.
The atomic structures resulting from X-ray crystallography are crucial for understanding the biochemical and biophysical roles of a macromolecule in cellular function and disease. This understanding comes through the study of physiochemical interactions between molecules, as well as the study of conformational changes and chemical catalysis.
X-ray crystallography has been used in major scientific advances during the past century — it is the means by which the molecular structures of DNA, hemoglobin, ion channels and RNA polymerase were determined. Additionally, nearly all recent Food and Drug Administration-approved small-molecule therapeutics depended upon crystallographic structures for decision-making during drug discovery and development.
Crystallography at Mayo Clinic
Collaborations in the Structural Biology Facility at Mayo Clinic are using crystallography for studies related to rational therapeutic drug design, alterations in supramolecular structure, enzyme mechanisms, and protein and nucleic acid recognition.