Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Proteins, like many molecules, can be prompted to form crystals when placed in the appropriate conditions. In order to crystallize a protein, the purified protein undergoes slow precipitation from an aqueous solution. As a result, individual protein molecules align themselves in a repeating series of unit cells by adopting a consistent orientation. The crystalline lattice that forms is held together by noncovalent interactions. The importance of protein crystallization is that it serves as the basis for X-ray crystallography, wherein a crystallized protein is used to determine the protein's three-dimensional structure via X-ray diffraction. In 1934, John Desmond Bernal and his student Dorothy Hodgkin discovered that protein crystals surrounded by their mother liquor gave better diffraction patterns than dried crystals. Using pepsin, they were the first to discern the diffraction pattern of a wet, globular protein.

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