Author: Tian, Xinsheng; Feng, Youjun; Zhao, Tiezhu; Peng, Hao; Yan, Jinghua; Qi, Jianxun; Jiang, Fan; Tian, Kegong; Gao, Feng
Title: Molecular cloning, expression, purification and crystallographic analysis of PRRSV 3CL protease Cord-id: 4yxda0mf Document date: 2007_7_28
ID: 4yxda0mf
Snippet: 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 Ã… resolution and belong to space group C2, with unit-cell parameters a = 112.31, b = 48.34, c = 42.88 Ã…,
Document: 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 Å(3) Da(−1) and 50.61%, respectively, for one molecule in the asymmetric unit.
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