Cloning, purification, crystallization and preliminary X‐ray studies of the putative type VI secretion immunity protein Tli5 (PA5088) from Pseudomonas aeruginosa. Issue 7 (1st July 2014)

• Record Type: Journal Article
• Authors: Chen, Zhen; Gao, Zengqiang; Hu, Haidai; Xu, Jianhua; Zhang, Heng; Dong, Yuhui
• Is Part Of: Acta crystallographica. Volume 70:Issue 7(2014:Jul.)
• Page Start: 903
• Page End: 905
• Publication Date: 2014-07-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14010164
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The putative protein PA5089 from <italic>Pseudomonas aeruginosa</italic> 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 <italic>P</italic>2₁, with unit‐cell parameters <italic>a</italic> = 64.002, <italic>b</italic> = 104.744, <italic>c</italic> = 90.168 Å.</p> </abstract>