Protein interactions and complexes have recently been the subject of great interest. Methods like the two-hybrid system or affinity purifications have identified thousands of interactions and hundreds of complexes, providing a rich source of information related to biological function. A deeper understanding of the function of a protein complex comes from knowledge of its three-dimensional (3D) structure, and such complexes are now the focus of much of experimental structural biology. However, methodological limitations mean that atomic resolution structures for complexes of even two proteins often require years of work. This has led to an information gap between complexes known experimentally and those with 3D structures. Here, we will show how a combination of computational and experimental methods can partly dodge these problems to provide a substantial view of complex cellular structures.
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