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...
Saved in:
Published in | Journal of molecular biology Vol. 233; no. 4; pp. 787 - 788 |
---|---|
Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford
Elsevier Ltd
20.10.1993
Elsevier |
Subjects | |
Online Access | Get full text |
Cover
Loading…
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. |
---|---|
Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0022-2836 1089-8638 |
DOI: | 10.1006/jmbi.1993.1554 |