Zhilin Ren

Publications (3)1.01 Total impact

• Article: The newly emerged SARS-Like coronavirus HCoV-EMC also has an "Achilles' heel": current effective inhibitor targeting a 3C-like protease.

  Zhilin Ren, Liming Yan, Ning Zhang, Yu Guo, Cheng Yang, Zhiyong Lou, Zihe Rao
  Protein & Cell 04/2013; 4(4):248-50.
• Article: Purification, crystallization and preliminary X-ray analysis of nonstructural protein 2 (nsp2) from avian infectious bronchitis virus.

  Kun Yu, Zhenhua Ming, Yuanyuan Li, Cheng Chen, Zehua Bao, Zhilin Ren, Bofeng Liu, Wei Tao, Zihe Rao, Zhiyong Lou
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  ABSTRACT: Avian infectious bronchitis virus (IBV) is a member of the group III coronaviruses, which differ from the other groups of coronaviruses in that they do not encode the essential pathogenic factor nonstructural protein 1 (nsp1) and instead start with nsp2. IBV nsp2 is one of the first replicase proteins to be translated and processed in the viral life cycle; however, it has an entirely unknown function. In order to better understand the structural details and functional mechanism of IBV nsp2, the recombinant protein was cloned, overexpressed in Escherichia coli, purified and crystallized. The crystals diffracted to 2.8 Å resolution and belonged to space group P2(1), with unit-cell parameters a = 57.0, b = 192.3, c = 105.7 Å, β = 90.8°. Two molecules were found in the asymmetric unit; the Matthews coefficient was 3.9 Å(3) Da(-1), corresponding to a solvent content of 68.2%.
  Acta Crystallographica Section F Structural Biology and Crystallization Communications 06/2012; 68(Pt 6):716-9. · 0.51 Impact Factor
• Article: Expression, crystallization and preliminary crystallographic study of the C-terminal half of nsp2 from SARS coronavirus.

  Yuanyuan Li, Zhilin Ren, Zehua Bao, Zhenhua Ming, Xuemei Li
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  ABSTRACT: SARS coronavirus (SARS-CoV) is the aetiological agent of the highly infectious severe acute respiratory syndrome (SARS). To gain a better understanding of SARS-CoV replication and transcription proteins, a preliminary X-ray crystallographic study of the C-terminal domain of SARS-CoV nonstructural protein 2 (nsp2) is reported here. The C-terminal domain of SARS-CoV nsp2 was cloned, overexpressed, purified and crystallized using polyethylene glycol 5000 monomethyl ether as the precipitant; the crystals diffracted to 2.5 Å resolution. The crystals belonged to space group P6(5), with unit-cell parameters a=b=112.8, c=91.1 Å, α=β=90, γ=120°. One molecule is assumed to be present per asymmetric unit, which gives a Matthews coefficient of 2.89 Å3 Da(-1) and a solvent content of 56.2%.
  Acta Crystallographica Section F Structural Biology and Crystallization Communications 07/2011; 67(Pt 7):790-3. · 0.51 Impact Factor