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 A resolution using synchrotron radiation. The crystals belong to the tetragonal space group I4, with unit-cell parameters a = b = 145.79, c = 130.98 A. The asymmetric unit contains a tetramer, giving a crystal Volume per protein mass (V(M)) of 2.13 A(3) Da(-1) and a solvent content of 42.3%.
Ahn
Hyung Jun
HJ
Structural Proteomics Laboratory, School of Chemistry and Molecular Engineering, Seoul National University, Seoul 151 742, South Korea.
Yang
Jin Kuk
JK
Lee
Byung Il
BI
Yoon
Hye Jin
HJ
Kim
Hyung Wook
HW
Suh
Se Won
SW
D003460:Crystallization; D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000096:biosynthesis / Q000235:genetics; D004926:Escherichia coli / Q000378:metabolism; D016480:Helicobacter pylori / Q000201:enzymology*; D008027:Light; D019761:Phosphorus-Oxygen Lyases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D012542:Scattering, Radiation
D018076:DNA, Complementary; C019895:chorismate synthase; D019761:Phosphorus-Oxygen Lyases