We aim to rapidly express several new constructs which will make the CFTR protein more stable and therefore, crystallizable. The main roadblocks preventing successful crystallization of CFTR for anyone are 1) the amount of protein that we can express and purify and 2) the stability of purified CFTR. Initial research performed by our team has clearly demonstrated several post-translational sites that, if mutated to a different amino acid could result in a higher percentage of properly folded CFTR and more stable CFTR subsequent to purification. We plan to quickly explore as many as 40 new constructs which have been shown to improve both of these roadblocks. Within months we would be able to express and purify CFTR protein for all of these constructs. The purified protein could then be used to screen approximately 1,200 conditions for each construct. The improved expression and stability could result in one or more of these constructs resulting in crystals from which we can ultimately determine the atomic structure of CFTR. The structure would enable several key aspects connected with the development of a new pharmaceutical that could prolong the lives of CF patients or even allow them to live a full life.