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....
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-03, Vol.59 (3), p.569-571 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
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| creator | Ahn, Hyung Jun Yang, Jin Kuk Lee, Byung Il Yoon, Hye Jin Kim, Hyung Wook Suh, Se Won |
| description | 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%. |
| doi_str_mv | 10.1107/S090744490300009X |
| format | Article |
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Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>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. 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| ispartof | Acta crystallographica. Section D, Biological crystallography., 2003-03, Vol.59 (3), p.569-571 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | 5-enolpyruvylshikimate 3-phosphate aroC chorismate synthase Crystallization Crystallography, X-Ray DNA, Complementary - biosynthesis DNA, Complementary - genetics Escherichia coli - metabolism Helicobacter pylori Helicobacter pylori - enzymology Light Phosphorus-Oxygen Lyases - chemistry Phosphorus-Oxygen Lyases - genetics Phosphorus-Oxygen Lyases - isolation & purification Scattering, Radiation shikimate pathway |
| title | Crystallization and preliminary X-ray crystallographic studies of chorismate synthase from Helicobacter pylori |
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