This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We are studying a novel viral protease. This protease is a self-processing type, and it cleaves itself at its N- and C- terminus. It has a unique type of active site, not found in any other group of viral proteases. Our goal is to solve the structure of such viral protease, in order to gain insights into the details of its mechanisms. In addition, these proteases are potential drug targets, considering that the virus infects farmed fish. We have Seleno-Met crystals of the protease, that belong to space group P6122. These crystals diffract to better than 2.5A at the home source. We also have native crystals of P6122, that diffract to 2A at the home source. in addition we have some Seleno-Met triclinic crystals of the same protease. The strategy for solving the structure is a MAD / SAD solution. We hope that one of these approaches will allow us to solve the structure of these viral proteases. We are also including 2 larger native crystals (P6122) for a high resolution data set, if possible.
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