| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1929436 | Biochemical and Biophysical Research Communications | 2012 | 5 Pages |
Di- and oligopeptide- binding protein OppAs play important roles in solute and nutrient uptake, sporulation, biofilm formation, cell wall muropeptides recycling, peptide-dependent quorum-sensing responses, adherence to host cells, and a variety of other biological processes. Soluble OppA from Thermoanaerobacter tengcongensis was expressed in Escherichia coli. The protein was found to be >95% pure with SDS–PAGE after a series of purification steps and the purity was further verified by mass spectrometry. The protein was crystallized using the sitting-drop vapour-diffusion method with PEG 400 as the precipitant. Crystal diffraction extended to 2.25 Å. The crystal belonged to space group C2221, with unit-cell parameters of a = 69.395, b = 199.572, c = 131.673 Å, and α = β = γ = 90°.
► We truncated the signal peptide of OppATTE0054 to make it express in Escherichia coli as a soluble protein. ► Crystals of OppATTE0054 were grown by sitting-drop vapor diffusion method. ► The crystal of OppATTE0054 diffracted to 2.25 Å.
