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Cloning, purification, crystallization and preliminary X-ray studies of the putative type VI secretion immunity protein Tli5 (PA5088) from Pseudomonas aeruginosa.

Authors
  • Chen, Zhen
  • Gao, Zengqiang
  • Hu, Haidai
  • Xu, Jianhua
  • Zhang, Heng
  • Dong, Yuhui
Type
Published Article
Journal
Acta crystallographica. Section F, Structural biology communications
Publication Date
Jul 01, 2014
Volume
70
Issue
Pt 7
Pages
903–905
Identifiers
DOI: 10.1107/S2053230X14010164
PMID: 25005085
Source
Medline
Keywords
License
Unknown

Abstract

The putative protein PA5089 from Pseudomonas aeruginosa has recently been identified as a Tle5 phospholipase effector from a type VI secretion system (T6SS), and its toxicity can be neutralized by the cognate immunity protein Tli5 (PA5088). Here, the expression, purification, crystallization and preliminary crystallographic analysis of PA5088 are reported. X-ray diffraction data were collected from selenomethionine-derivatized PA5088 crystals to a resolution of 2.55 Å. The crystals belonged to space group P2₁, with unit-cell parameters a=64.002, b=104.744, c=90.168 Å.

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