Crystallization and preliminary X-ray crystallographic studies of chorismate synthase from Helicobacter pylori

Chorismate synthase (EC 4.6.1.4) catalyzes the transformation of 5‐­enolpyruvylshikimate 3‐phosphate to chorismate in the last step of the shikimate pathway. Chorismate synthase from Helicobacter pylori fused with an eight‐residue C‐terminal tag was overexpressed in soluble form in Escherichia coli. It was crystallized at 296 K using polyethylene glycol 400 as a precipitant. A set of X‐ray diffraction data was collected to 2.5 Å resolution using synchrotron radiation. The crystals belong to the tetragonal space group I4, with unit‐cell parameters a = b = 145.79, c = 130.98 Å. The asymmetric unit contains a tetramer, giving a crystal volume per protein mass (VM) of 2.13 Å3 Da−1 and a solvent content of 42.3%.