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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Rapid X-ray diffraction analysis of HIV-1 protease-inhibitor complexes: inhibitor exchange in single crystals of the bound enzyme.

The ability to replace an inhibitor bound to the HIV-1 protease in single crystals with other potent inhibitors offers the possibility of investigating a series of protease inhibitors rapidly and conveniently with the use of X-ray crystallography. This approach affords a fast turnaround of structural information for iterative rational drug designs and obviates the need for studying the complex structures by co-crystallization. The replacement approach has been successfully used with single crystals of the HIV-1 protease complexed with a weak inhibitor. The structures of the complexes obtained by the replacement method are similar to those determined by co-crystallization.[1]

References

  1. Rapid X-ray diffraction analysis of HIV-1 protease-inhibitor complexes: inhibitor exchange in single crystals of the bound enzyme. Munshi, S., Chen, Z., Li, Y., Olsen, D.B., Fraley, M.E., Hungate, R.W., Kuo, L.C. Acta Crystallogr. D Biol. Crystallogr. (1998) [Pubmed]
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