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Updated: Jun 2, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Purification, crystallization and preliminary X-ray crystallographic analysis of the putative Vibrio parahaemolyticus
Inci Aydin1, Alexandra Dimitropoulos, Shih Hsun Chen
1Department of Microbiology, Monash University, Clayton, Victoria 3800, Australia.
Abstract:
Vibrio parahaemolyticus is a human pathogen associated with gastroenteritis caused by the ingestion of contaminated raw seafood. V. parahaemolyticus is able to survive exposure to low temperatures typical of those used for the refrigeration of foods by entering a viable but nonculturable (VBNC) state. The VBNC cells can regain culturability and renewed ability to cause infection upon temperature upshift. The resuscitation-promoting factor protein (Rpf, YeaZ) plays a key role in reactivation of growth. Crystals of V. parahaemolyticus YeaZ have been grown using the hanging-drop vapour-diffusion method with polyethylene glycol as a precipitating agent. The crystals belonged to the primitive monoclinic space group P2(1), with unit-cell parameters a = 81.7, b = 63.8, c = 82.3 Å, β = 105° and four subunits in the asymmetric unit. A complete X-ray diffraction data set was collected from a single crystal to 3.1 Å resolution.

