Molecular cloning, expression, purification and crystallographic analysis of PRRSV 3CL protease
3CL protease, a viral chymotrypsin‐like proteolytic enzyme, plays a pivotal role in the transcription and replication machinery of many RNA viruses, including porcine reproductive and respiratory syndrome virus (PRRSV). In this study, the full‐length 3CL protease from PRRSV was cloned and overexpressed in Escherichia coli. Crystallization experiments yielded crystals that diffracted to 2.1 Å resolution and belong to space group C2, with unit‐cell parameters a = 112.31, b = 48.34, c = 42.88 Å, β = 109.83°. The Matthews coefficient and the solvent content were calculated to be 2.49 Å3 Da−1 and 50.61%, respectively, for one molecule in the asymmetric unit.
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