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

U G Wagner; H Bergler; S Fuchsbichler; F Turnowsky; G Högenauer; C Kratky

doi:10.1006/jmbi.1994.1636

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

J Mol Biol. 1994 Oct 14;243(1):126-7. doi: 10.1006/jmbi.1994.1636.

Authors

U G Wagner¹, H Bergler, S Fuchsbichler, F Turnowsky, G Högenauer, C Kratky

Affiliation

¹ Institut für Physikalische Chemie, Karl-Franzens-Universität Graz, Austria.

PMID: 7932735
DOI: 10.1006/jmbi.1994.1636

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Crystallography, X-Ray
Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)
Escherichia coli / enzymology*
Escherichia coli Proteins
Fatty Acid Synthase, Type II
Fatty Acid Synthases / chemistry*
Oxidoreductases / chemistry*

Substances

Escherichia coli Proteins
Oxidoreductases
Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)
fabI protein, E coli
Fatty Acid Synthases
Fatty Acid Synthase, Type II