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Cloning, purification, crystallization and preliminary X-ray studies of flagellar hook scaffolding protein FlgD from Pseudomonas aeruginosa PAO1.

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).

SUBMITTER: Luo M

PROVIDER: S-EPMC2720336 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature

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Cloning, purification, crystallization and preliminary X-ray studies of flagellar hook scaffolding protein FlgD from Pseudomonas aeruginosa PAO1.

Luo Miao M Niu Siqiang S Yin Yibing Y Huang Ailong A Wang Deqiang D

Acta crystallographica. Section F, Structural biology and crystallization communications 20090725 Pt 8

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 analys ...[more]

PMID: 19652342

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