Crystallization and preliminary X-ray diffraction studies of the enoyl-ACP reductase from Escherichia coli. 1994

U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
Institut für Physikalische Chemie, Karl-Franzens-Universität Graz, Austria.

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.

UI MeSH Term Description Entries
D010088 Oxidoreductases The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D003460 Crystallization The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Crystalline Polymorphs,Polymorphism, Crystallization,Crystal Growth,Polymorphic Crystals,Crystal, Polymorphic,Crystalline Polymorph,Crystallization Polymorphism,Crystallization Polymorphisms,Crystals, Polymorphic,Growth, Crystal,Polymorph, Crystalline,Polymorphic Crystal,Polymorphisms, Crystallization,Polymorphs, Crystalline
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D050753 Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) An NAD-dependent enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein]. It has a preference for acyl groups with a carbon chain length between 4 to 16. Enoyl(Acyl-Carrier-Protein) Reductase (NADH),NADH-Dependent Enoyl-ACP Reductase,NADH-Enoyl ACP Reductase,ACP Reductase, NADH-Enoyl,Enoyl-ACP Reductase, NADH-Dependent,NADH Dependent Enoyl ACP Reductase,NADH Enoyl ACP Reductase,Reductase, NADH-Dependent Enoyl-ACP,Reductase, NADH-Enoyl ACP
D054889 Fatty Acid Synthase, Type II The form of fatty acid synthase complex found in BACTERIA; FUNGI; and PLANTS. Catalytic steps are like the animal form but the protein structure is different with dissociated enzymes encoded by separate genes. It is a target of some ANTI-INFECTIVE AGENTS which result in disruption of the CELL MEMBRANE and CELL WALL. Fatty Acid Synthase II,Fatty Acid Synthetase Complex, Type II,FAS-II Synthase,Fatty Acid Synthase Type II,Fatty Acid Synthase, Bacterial, Plant, and Fungi Form,FAS II Synthase,Synthase, FAS-II
D018360 Crystallography, X-Ray The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) X-Ray Crystallography,Crystallography, X Ray,Crystallography, Xray,X Ray Crystallography,Xray Crystallography,Crystallographies, X Ray,X Ray Crystallographies
D029968 Escherichia coli Proteins Proteins obtained from ESCHERICHIA COLI. E coli Proteins
D064429 Fatty Acid Synthases Enzymes that catalyze the synthesis of FATTY ACIDS from acetyl-CoA and malonyl-CoA derivatives. Fatty Acid Synthase,Fatty Acid Synthetases,Acid Synthase, Fatty,Acid Synthases, Fatty,Synthase, Fatty Acid,Synthetases, Fatty Acid

Related Publications

U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
September 2000, Acta crystallographica. Section D, Biological crystallography,
U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
June 1983, The Journal of biological chemistry,
U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
March 2007, Acta crystallographica. Section F, Structural biology and crystallization communications,
U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
February 2002, Acta crystallographica. Section D, Biological crystallography,
U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
October 2003, Acta crystallographica. Section D, Biological crystallography,
U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
March 1998, Acta crystallographica. Section D, Biological crystallography,
U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
December 2014, Acta crystallographica. Section F, Structural biology communications,
U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
September 2005, Acta crystallographica. Section F, Structural biology and crystallization communications,
U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
August 1989, The Journal of biological chemistry,
U G Wagner, and H Bergler, and S Fuchsbichler, and F Turnowsky, and G Högenauer, and C Kratky
September 2003, Acta crystallographica. Section D, Biological crystallography,
Copied contents to your clipboard!