Protein crystallography

Protein crystallography determines atomic structures of proteins by analyzing how X-rays or other radiation diffract from ordered protein crystals.

X-ray crystallography: A method for determining atomic structures by analyzing X-ray diffraction from crystalline materials. Protein crystallography most often uses this broader diffraction method.
Protein: A biological macromolecule made of one or more chains of amino acids folded into a specific structure. Protein crystallography seeks the three-dimensional arrangements of these molecules.
Enzyme mechanism: The sequence of molecular events by which an enzyme converts substrates into products. Structures can reveal active-site arrangements that support proposed catalytic steps.
Cryogenic electron microscopy: A structural imaging method that reconstructs macromolecules from electron micrographs of rapidly frozen samples. It can determine protein structures without requiring ordered crystals.
Max Perutz: An Austrian-born British scientist who pioneered protein crystallography and determined the structure of hemoglobin. His long effort established methods for solving complex protein crystals.
Bragg's law: A relation connecting diffraction angles and wavelengths to spacing between crystal planes. It converts measured diffraction angles into constraints on crystal structure.
Protein folding: The physical process by which a protein chain adopts a three-dimensional structure. The folded structure is the object that crystallographic measurements aim to reveal.
Structure-based drug design: Drug discovery guided by the three-dimensional structures of biological targets and their binding sites. Protein crystal structures can show how candidate compounds occupy a target site.
Nuclear magnetic resonance spectroscopy: A method that uses nuclear magnetic resonance signals to study molecular structures and dynamics, often in solution. It can reveal protein structures in solution rather than in a crystal lattice.
John Kendrew: A British biochemist who determined the first atomic structure of a protein, myoglobin. His work demonstrated that protein crystal diffraction could yield a detailed molecular structure.

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