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The periplasmic sensing domain of Vibrio fischeri chemoreceptor protein A (VfcA): cloning, purification and crystallographic analysis.

ABSTRACT: Flagella-mediated motility and chemotaxis towards nutrients are important characteristics of Vibrio fischeri that play a crucial role in the development of its symbiotic relationship with its Hawaiian squid host Euprymna scolopes. The V. fischeri chemoreceptor A (VfcA) mediates chemotaxis toward amino acids. The periplasmic sensory domain of VfcA has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 3350 as a precipitating agent. The crystals belonged to space group P1, with unit-cell parameters a = 39.9, b = 57.0, c = 117.0?Å, ? = 88.9, ? = 80.5, ? = 89.7°. A complete X-ray diffraction data set has been collected to 1.8?Å resolution using cryocooling conditions and synchrotron radiation.

SUBMITTER: Salah Ud-Din AI

PROVIDER: S-EPMC4854566 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature

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The periplasmic sensing domain of Vibrio fischeri chemoreceptor protein A (VfcA): cloning, purification and crystallographic analysis.

Salah Ud-Din Abu Iftiaf Md AI Roujeinikova Anna A

Acta crystallographica. Section F, Structural biology communications 20160422 Pt 5

Flagella-mediated motility and chemotaxis towards nutrients are important characteristics of Vibrio fischeri that play a crucial role in the development of its symbiotic relationship with its Hawaiian squid host Euprymna scolopes. The V. fischeri chemoreceptor A (VfcA) mediates chemotaxis toward amino acids. The periplasmic sensory domain of VfcA has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 3350 as a precipitating agent. The crystals belonged to spa ...[more]

PMID: 27139830

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