Abstract
Extracellular proteins and receptor ectodomain fragments remain to be challenging targets for X-ray crystallography, due to the difficulties associated with the recombinant production as well as their intrinsic interdomain flexibility. We have determined crystal structures of the αIIbβ3 integrin headpiece fragment in complex with therapeutic antagonists. Unconventional tricks exploited during the course of the crystallization, including usage of a carbohydrate processing-deficient cell line, a“clasping”tag, extensive protease polishing, and the use of Fab fragment to rigidify the complex, are described.
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