Traditional structural biology techniques, which usually target particular proteins based on their biological significance, have been superseded by structural genomics. Rather, the goal of structural genomics is to systematically examine protein structures in three dimensions across the entire genome. This methodology entails the high-throughput synthesis, purification, and characterization of proteins, succeeded by the application of methods such as cryo-electron microscopy, NMR spectroscopy, or X-ray crystallography to determine their structural composition.

Structural genomics

One of the key goals of structural genomics is to create a comprehensive structural library that covers a significant portion of an organism's proteome. This library can provide valuable insights into the overall structural organization of proteins within an organism, as well as their functional relationships and evolutionary histories. By comparing protein structures across different species, structural genomics can also help identify conserved structural motifs and domains that are important for protein function.

Most structural genomics efforts create structural data, which is then made publically available through databases such as the Protein Data Bank (PDB). The scientific community can collaborate and share data more easily thanks to this open-access strategy, which also speeds up research in fields like systems biology, protein engineering, and drug discovery by allowing scientists to investigate novel theories.

The Protein Data Bank (PDB) file containing the atomic coordinates of 2PDD (Acyltransferase)

With broad ramifications for biology, medicine, and innovation, structural genomics is a potent tool for expanding our knowledge of protein structure and function on a genome-wide scale.


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