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New tools have helped to overcome some problems that have plagued the field. For example, the high degree of identity among the active sites of many of the PDEs has made them challenging targets for identification of selective inhibitors. This problem is being addressed by the use of high throughput screening and X-ray crystallography. In particular the solution of several PDE catalytic domain crystal structures in the presence of drugs has yielded crucial information on the active sites of these enzymes and allowed rational design to improve inhibitor potency and selectivity. Both high throughput screening and crystallization are now able to be performed efficiently with robotics, further decreasing the cost and increasing the speed with which PDE selective inhibitors can be discovered. Unfortunately, much less effort has gone into identification of activators of PDEs although much of the same technology could be applied. 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