Rapid X-ray diffraction analysis of HIV-1 protease–inhibitor complexes: inhibitor exchange in single crystals of the bound enzyme
Acta Crystallographica Section D
Volume 54, Issue 5, pages 1053–1060, September 1998
How to Cite
Munshi, S., Chen, Z., Li, Y., Olsen, D. B., Fraley, M. E., Hungate, R. W. and Kuo, L. C. (1998), Rapid X-ray diffraction analysis of HIV-1 protease–inhibitor complexes: inhibitor exchange in single crystals of the bound enzyme. Acta Cryst. D, 54: 1053–1060. doi: 10.1107/S0907444998003588
- Cited By
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.