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Expression, purification, crystallization and preliminary crystallographic analysis of PA3885 (TpbA) from Pseudomonas aeruginosa PAO1 by Wen Yang; Kan Li; Yuwei Bai; Ruimin Zhou; Weihong Zhou; Mark Bartlam is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Biofilms are important in cell communication and growth in most bacteria and are also responsible for most human clinical infections and diseases. Quorum-sensing systems have been identified to be crucial for biofilm formation and regulation. PA3885 (TpbA), a tyrosine phosphatase, is reported to convert extracellular quorum-sensing signals into internal gene-cascade reactions that result in reduced biofilm formation in the opportunistic pathogen Pseudomonas aeruginosa. Here, PA3885 from P. aeruginosa PAO1 was expressed, purified and crystallized. Single crystals were studied by X-ray crystallography and native diffraction data were collected to 2.8 Å resolution. These crystals were determined to belong to space group C2. It was not possible to conclusively determine the number of proteins in the asymmetric unit from the preliminary X-ray diffraction data analysis alone and attempts to determine the crystal structure of PA3885 are currently under way.

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Author

Wen Yang; Kan Li; Yuwei Bai; Ruimin Zhou; Weihong Zhou; Mark Bartlam

Publisher

John Wiley and Sons; International Union of Crystallography; John Wiley and Sons Ltd; International Union of Crystallography (IUCr) (ISSN 1744-3091)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)