title: 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).
authors: Key Laboratory of Molecular Biology on Infectious Disease, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, People's Republic of China.
authors: Miao
authors: M
authors: Luo
authors: Siqiang
authors: S
authors: Niu
authors: Yibing
authors: Y
authors: Yin
authors: Ailong
authors: A
authors: Huang
authors: Deqiang
authors: D
authors: Wang
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins