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

Abu Iftiaf Md Salah Ud-Din, Anna Roujeinikova

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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 hangingdrop 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 A, a = 88.9, B = 80.5, y = 89.7 . A complete X-ray diffraction data set has been collected to 1.8 A ? resolution using cryocooling conditions and synchrotron radiation.
Original languageEnglish
Pages (from-to)382-385
Number of pages4
JournalActa Crystallographica Section F: Structural Biology Communications
VolumeF72
Issue numberPart 5
DOIs
Publication statusPublished - 1 May 2016

Keywords

  • bacterial chemotaxis
  • methyl-accepting protein
  • receptor
  • sensing domain

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