Crystallization and Preliminary X-ray Diffraction Studies of Bacillus stearothermophilus Farnesyl Diphosphate Synthase Expressed in Escherichia coli

Thermostable farnesyl diphosphate synthase (EC 2.5.1.10) from Bacillus stearothermophilus, which was overexpressed in Escherichia coli, has been crystallized by the vapor-diffusion procedure. Tetragonal crystals were obtained using ammonium sulfate as a precipitant. The crystals diffracted X-rays to...

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Published inJournal of molecular biology Vol. 233; no. 4; pp. 787 - 788
Main Authors Nakane, Hiroyuki, Koyama, Tanetoshi, Obata, Shusei, Osabe, Masami, Takeshita, Ayumi, Nishino, Tokuzo, Ogura, Kyozo, Miki, Kunio
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 20.10.1993
Elsevier
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Summary:Thermostable farnesyl diphosphate synthase (EC 2.5.1.10) from Bacillus stearothermophilus, which was overexpressed in Escherichia coli, has been crystallized by the vapor-diffusion procedure. Tetragonal crystals were obtained using ammonium sulfate as a precipitant. The crystals diffracted X-rays to about 3 Å resolution. The diffraction pattern indicated that the space group is I4122 with unit-cell dimensions of a = b = 114 Å and c = 247 Å. It is thought that the asymmetric unit comprises two or three molecules of farnesyl diphosphate synthase.
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ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1993.1554