Crystallization and preliminary X-ray crystallographic analysis of a ytfG gene product from Escherichia coli.
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%.
Kim
In-Kwon
IK
Laboratory of Biophysics, School of Biological Sciences, Seoul National University, Seoul 151-742, South Korea.
Yim
Hyung-Soon
HS
Kim
Dong-Won
DW
Kim
Young-Min
YM
Lee
Heung-Soo
HS
Cha
Sun-Shin
SS
Kang
Sa-Ouk
SO
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
D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D012997:Solvents; D011092:Polyethylene Glycols; D010088:Oxidoreductases; D009247:NADH, NADPH Oxidoreductases; C491821:ytfG protein, E coli