Send to

Choose Destination
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):637-9. doi: 10.1107/S1744309111011286. Epub 2011 Apr 28.

Protein expression, crystallization and preliminary X-ray crystallographic studies of LidA from Legionella pneumophila.

Author information

State Key Lab of Protein and Plant Gene Research, Peking University, Beijing 100871, People's Republic of China.


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.

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for International Union of Crystallography Icon for PubMed Central
Loading ...
Support Center