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  • Title: Cloning, purification, crystallization and preliminary X-ray studies of flagellar hook scaffolding protein FlgD from Pseudomonas aeruginosa PAO1.
    Author: Luo M, Niu S, Yin Y, Huang A, Wang D.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2009 Aug 01; 65(Pt 8):795-7. PubMed ID: 19652342.
    Abstract:
    FlgD regulates the assembly of the hook cap structure to prevent leakage of hook monomers into the medium and hook monomer polymerization and also plays a role in determination of the correct hook length, with the help of the FliK protein. In order to better elucidate the functions of FlgD in flagellar hook biosynthesis, the three-dimensional structure of FlgD is being determined by X-ray crystallography. Here, the expression, purification, crystallization and preliminary crystallographic analysis of FlgD from P. aeruginosa are reported. The crystal belonged to space group I222 and diffracted to a resolution of 2.5 A, with unit-cell parameters a = 116.47, b = 118.71, c = 118.85 A. The crystals are most likely to contain three molecules in the asymmetric unit, with a V(M) value of 2.73 A(3) Da(-1).
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