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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
Author(s) -
Chen Zhen,
Gao Zengqiang,
Hu Haidai,
Xu Jianhua,
Zhang Heng,
Dong Yuhui
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14010164
Subject(s) - pseudomonas aeruginosa , crystallization , secretion , cloning (programming) , effector , immunity , biology , chemistry , microbiology and biotechnology , immune system , biochemistry , bacteria , genetics , organic chemistry , computer science , programming language
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 P 2 1 , with unit‐cell parameters a = 64.002, b = 104.744, c = 90.168 Å.