Macromolecular Structure Determination by X‐ray Crystallography

Abstract X‐ray diffraction is a well‐established method to elucidate the atomic structure of single‐crystal macromolecules. An image of the macromolecule forming the crystal cannot be directly recorded as the X‐ray phase information is lost during the diffraction experiment. Through systematic variation of the chemical content in the crystal and/or through small changes in the wavelength of the incident X‐ray beam, however, a sharp image can be reconstituted computationally. Within the Protein Data Bank, the vast majority of three‐dimensional structures available have been determined using X‐ray diffraction. These structures are used to correlate macromolecular structure with function, to study molecular mechanisms and serve as templates for structure‐based drug design of novel therapeutic agents for the treatment of many diseases.