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 language | English |
|---|---|
| Pages (from-to) | 382-385 |
| Number of pages | 4 |
| Journal | Acta Crystallographica Section F: Structural Biology Communications |
| Volume | F72 |
| Issue number | Part 5 |
| DOIs | |
| Publication status | Published - 1 May 2016 |
Keywords
- bacterial chemotaxis
- methyl-accepting protein
- receptor
- sensing domain
Equipment
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Monash Macromolecular Crystallisation Platform (MMCP)
Kong, G. (Operator)
Faculty of Medicine Nursing and Health Sciences Research PlatformsFacility/equipment: Facility