Protein Crystallography / Macromolecular Crystallography

Crystalline samples of proteins, DNA, RNA or other large molecules interact with X-rays to produce diffraction patterns. Refocusing of the diffraction pattern is done mathematically, to produce an average picture of the constituent molecules of the crystal.

Various techniques give different and complementary information about protein structure and function. The primary structure (sequence) of a protein is determined by biochemical methods. The secondary structure distribution (alpha helices, beta sheets and random turns) might be determined with spectroscopic techniques such as Circular Dichroism. To determine the tertiary (3D) structure, detailed high resolution information is required about the arrangement of atoms within a protein or macromolecule. The main method used is X-ray diffraction, which enables the recording of information down to atomic resolution (1.0 Å).

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