engleski

Structural studies of FlgD - flagella hook capping protein from Helicobacter pylori

FlgD plays an important role in H. pylori virulence, owing to its role in forming the hook cap component. In order to clarify the structural and functional properties of this H. pylori virulence factor we performed cloning, purification, crystallization and X-ray analysis studies. FlgD was overexpressed in BL21 E. coli cells as a His-tagged protein at the C-terminus. Optimal expression conditions were established and recombinant FlgD was purified firstly by affinity chromatography and then by size-exclusion chromatography. Afterwards, FlgD was concentrated to 18 mg ml-1 and single crystals were grown at 293(2) K by the sitting drop vapor diffusion method using an automated crystallization platform (Oryx 8 robot). Diffraction data were collected at the beamline ID23-1 of the ESRF synchrotron facility (Grenoble, France) to the resolution of 2.75 Å.

H. pylori ; FlgD ; crystallization ; X-ray diffraction

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