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

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• 作者：Abu Iftiaf Md Salah Ud-Din and Anna Roujeinikova
• 关键词：bacterial chemotaxis ; receptor ; sensing domain ; methyl-accepting protein
• 刊名：Acta Crystallographica Section F
• 出版年：2016
• 出版时间：May 2016
• 年：2016
• 卷：72
• 期：5
• 页码：382-385
• 全文大小：394K
• ISSN：1744-3091

文摘

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, α = 88.9, β = 80.5, γ = 89.7°. A complete X-ray diffraction data set has been collected to 1.8 Å resolution using cryocooling conditions and synchrotron radiation.