title: Protein expression, crystallization and preliminary X-ray crystallographic studies of LidA from Legionella pneumophila.
abstract: LidA, a translocated substrate of the Legionella pneumophila Dot/Icm type IV secretion system, is associated with maintenance of bacterial integrity and interferes with the early secretory pathway. However, the precise mechanism of LidA in these processes remains elusive. To further investigate the structure and function of LidA, the full-length protein was successfully expressed in Escherichia coli and purified. LidA was crystallized using sitting-drop vapour diffusion and diffracted to a resolution of 2.75 Å. The crystal belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 57.5, b = 64.5, c = 167.3 Å, α = β = γ = 90°. There is one molecule per asymmetric unit.
authors.affiliation: State Key Lab of Protein and Plant Gene Research, Peking University, Beijing 100871, People's Republic of China.
authors.forename: Wenzhuang
authors.initials: W
authors.lastname: Zhu
authors.forename: Geng
authors.initials: G
authors.lastname: Meng
authors.forename: Yong
authors.initials: Y
authors.lastname: Liu
authors.forename: Feiyun
authors.initials: F
authors.lastname: Zhang
authors.forename: Xiaofeng
authors.initials: X
authors.lastname: Zheng
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D016952:Legionella pneumophila / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins