Ontology highlight
ABSTRACT:
SUBMITTER: Mao Q
PROVIDER: S-EPMC2330128 | biostudies-literature | 2007 Feb
REPOSITORIES: biostudies-literature
Mao Qilong Q Duax William L WL Umland Timothy C TC
Acta crystallographica. Section F, Structural biology and crystallization communications 20070117 Pt 2
The gene product of fabG from Aquifex aeolicus has been heterologously expressed in Escherichia coli. Purification of the protein took place using anion-exchange and size-exclusion chromatography and the protein was then crystallized. Diffraction data were collected to a maximum resolution of 1.8 A and the initial phases were determined by molecular replacement. The A. aeolicus FabG protein is a putative beta-ketoacyl-acyl carrier protein reductase. Structure-function studies of this protein are ...[more]