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  • Title: Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa PelD.
    Author: Marmont LS, Whitney JC, Robinson H, Colvin KM, Parsek MR, Howell PL.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2012 Feb 01; 68(Pt 2):181-4. PubMed ID: 22297994.
    Abstract:
    The production of the PEL polysaccharide in Pseudomonas aeruginosa requires the binding of bis-(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) to the cytoplasmic GGDEF domain of the inner membrane protein PelD. Here, the overexpression, purification and crystallization of a soluble construct of PelD that encompasses the GGDEF domain and a predicted GAF domain is reported. Diffraction-quality crystals were grown using the hanging-drop vapour-diffusion method. The crystals grew as flat plates, with unit-cell parameters a = 88.3, b = 114.0, c = 61.9 Å, α = β = γ = 90.0°. The PelD crystals exhibited the symmetry of space group P2(1)2(1)2 and diffracted to a minimum d-spacing of 2.2 Å. On the basis of the Matthews coefficient (V(M) = 2.29 Å(3) Da(-1)), it was estimated that two molecules are present in the asymmetric unit.
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