Crystallization and preliminary X-ray diffraction studies of the enoyl-ACP reductase from Escherichia coli.
A crystal of the FabI protein from Escherichia coli has been obtained from polyethylene glycol (M(r) = 400) solution with sodium citrate at pH 8.5, by the hanging-drop technique at 4 degrees C. The crystal belongs to the hexagonal space group P6(1)22 (or P6(5)22) with cell dimensions of a = b = 81.1 A and c = 331.5 A. There are two molecules in the asymmetric unit and the crystal diffracts to 2.5 A resolution.
Wagner
U G
UG
Institut für Physikalische Chemie, Karl-Franzens-Universität Graz, Austria.
Bergler
H
H
Fuchsbichler
S
S
Turnowsky
F
F
Högenauer
G
G
Kratky
C
C
D003460:Crystallization; D018360:Crystallography, X-Ray; D050753:Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D054889:Fatty Acid Synthase, Type II; D064429:Fatty Acid Synthases / Q000737:chemistry*; D010088:Oxidoreductases / Q000737:chemistry*
D029968:Escherichia coli Proteins; D010088:Oxidoreductases; D050753:Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); C493924:fabI protein, E coli; D064429:Fatty Acid Synthases; D054889:Fatty Acid Synthase, Type II