title: Crystallization and preliminary X-ray crystallographic analysis of a ytfG gene product from Escherichia coli.
abstract: The Escherichia coli ytfG gene product, with NAD(P)H:quinone oxidoreductase activity, was crystallized by the hanging-drop vapour-diffusion method at 296 K. A 1.78 A data set has been collected using synchrotron radiation at Pohang Light Source, South Korea. The crystal belongs to the primitive trigonal system, with unit-cell parameters a = b = 81.7, c = 76.8 A. Analysis of the packing density shows that the asymmetric unit probably contains one monomer, with a solvent content of 48.8%.
authors.affiliation: Laboratory of Biophysics, School of Biological Sciences, Seoul National University, Seoul 151-742, South Korea.
authors.forename: In-Kwon
authors.initials: IK
authors.lastname: Kim
authors.forename: Hyung-Soon
authors.initials: HS
authors.lastname: Yim
authors.forename: Dong-Won
authors.initials: DW
authors.lastname: Kim
authors.forename: Young-Min
authors.initials: YM
authors.lastname: Kim
authors.forename: Heung-Soo
authors.initials: HS
authors.lastname: Lee
authors.forename: Sun-Shin
authors.initials: SS
authors.lastname: Cha
authors.forename: Sa-Ouk
authors.initials: SO
authors.lastname: Kang
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D003593:Cytoplasm / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry*; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry*; D010088:Oxidoreductases / Q000737:chemistry; D011092:Polyethylene Glycols / Q000737:chemistry; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000737:chemistry; D012997:Solvents; D017356:Synchrotrons; D013696:Temperature
chemical_list: D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D012997:Solvents; D011092:Polyethylene Glycols; D010088:Oxidoreductases; D009247:NADH, NADPH Oxidoreductases; C491821:ytfG protein, E coli