Proper function of a-lytic protease requires the presence of its N-terminal pro region, which catalyzes an as yet unidentified step in the folding of this enzyme. In order to better understand the folding mechanism, we are using x-ray crystallography to determine the structure of the pro region, both by itself and in a complex with folded protease. We have engineered several mutants containing cysteines to facilitate the preparation of heavy atom derivatives for multiple isomorphous replacement.
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