• DOI:10.1126/science.1188383
• Corpus ID: 44583219

Protein crystal structures: quicker, cheaper approaches

@article{Collins1975ProteinCS,
  title={Protein crystal structures: quicker, cheaper approaches},
  author={Douglas M. Collins and F. A. Cotton and E. E. Jun. Hazen and Edgar F. Meyer and Carl N. Morimoto},
  journal={Science},
  year={1975},
  volume={190},
  pages={1047 - 1053}
}

• D. Collins, F. A. Cotton, +2 authors C. Morimoto
• Published 12 December 1975
• Chemistry
• Science

The use of x-ray diffraction methods to study crystals of biological macromolecules dates from 1934, when Bernal and Crowfoot (1) found that the diffraction patterns from crystals of the proteolytic enzyme pepsin were, in Hodgkin's words (2), "rich and full of detail." The potential for revealing the precise molecular structure of protein molecules inherent in such diffraction patterns remained unrealized until 1954, when M. F. Perutz, who had devoted his early career to the effort, showed that the "isomorphous" insertion of heavy atoms into the crystal lattice could provide phase information, after which J. C. Kendrew solved the structure of myoglobin and Perutz solved that of hemoglobin. In 1965 Phillips reported the first detailed structure of an enzyme, lysozyme, but perhaps more important was his demonstration that it is possible to study directly the binding of a substrate-like molecule at the active site. For details of the methods and references to the many contributions of others to the field, the authoritative reviews by Phillips (3) and North and Phillips (4) should be consulted. Today the crystal structures of more than 50 proteins and transfer ribonucleic acids are under investigation in laboratories throughout the world. Howevet, despite the wide applicability and success of the method, crystal structure determination for biological macromolecules remains time-consuming and expensive. It is