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中国生物工程杂志

China Biotechnology
China Biotechnology  2014, Vol. 34 Issue (5): 1-5    DOI: 10.13523/j.cb.20140501
    
The Expression, Purification and Studying for Crystallization of Subclone of Effector Protein LepB
Xu An-bi1,2, HUANG Lai-qiang1,2
1 School of Life Sciences, Tsinghua University, Beijing 100084, China;
2 Graduate School at Shenzhen, Tsinghua University, Shenzhen 518055, China
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Abstract  

The structural study of effector protein is important for studying thepathogenesis of legionella pneumophila. A construct for plasmid of LepB-PFastBac1-GST and 9 constructs for plasmids of LepB-truncation-PGEX-1-GST were successfully constructed and induced to express in insect cell or bacteria Bl21 (DE3),the obtained recombined protein was purified and crystallized by the vapor diffusion method. The crystal of the trunction of LepB -480-679 grows. The results Provide a basis for helping resolve the structure of LepB and further research work on the pathogenesis of legionella pneumophila.



Key wordsEffector protein      LepB      Crystallization     
Received: 19 March 2014      Published: 25 May 2014
ZTFLH:  Q816  
Cite this article:

Xu An-bi, HUANG Lai-qiang. The Expression, Purification and Studying for Crystallization of Subclone of Effector Protein LepB. China Biotechnology, 2014, 34(5): 1-5.

URL:

https://manu60.magtech.com.cn/biotech/10.13523/j.cb.20140501     OR     https://manu60.magtech.com.cn/biotech/Y2014/V34/I5/1


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