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Title: Purification, crystallization and preliminary X-ray diffraction analysis of enoyl-acyl carrier protein reductase (FabK) from Streptococcus mutans strain UA159. Author: Kim TO, Im DW, Jung HY, Kwon SJ, Heo YS. Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2012 Mar 01; 68(Pt 3):292-4. PubMed ID: 22442225. Abstract: A triclosan-resistant flavoprotein termed FabK is the sole enoyl-acyl carrier protein reductase in Streptococcus pneumoniae and Streptococcus mutans. In this study, FabK from S. mutans strain UA159 was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.40 Å resolution using a synchrotron-radiation source. The crystal belonged to space group P6(2), with unit-cell parameters a = b = 105.79, c = 44.15 Å. The asymmetric unit contained one molecule, with a corresponding V(M) of 2.05 Å(3) Da(-1) and a solvent content of 39.9%.[Abstract] [Full Text] [Related] [New Search]