Crystallization and X-ray studies of the DNA-binding domain of OmpR protein, a positive regulator involved in activation of osmoregulatory genes in Escherichia coli

H Kondo; T Miyaji; M Suzuki; S Tate; T Mizuno; Y Nishimura; I Tanaka

doi:10.1006/jmbi.1994.1032

Crystallization and X-ray studies of the DNA-binding domain of OmpR protein, a positive regulator involved in activation of osmoregulatory genes in Escherichia coli

J Mol Biol. 1994 Jan 14;235(2):780-2. doi: 10.1006/jmbi.1994.1032.

Authors

H Kondo¹, T Miyaji, M Suzuki, S Tate, T Mizuno, Y Nishimura, I Tanaka

Affiliation

¹ Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan.

PMID: 8289299
DOI: 10.1006/jmbi.1994.1032

Abstract

The OmpR protein of Escherichia coli is a positive regulator involved in the activation of expression of ompC and ompF genes encoding the major outer membrane protein OmpC and OmpF, respectively. The C-terminal half domain of OmpR (OmpR-C), which is responsible for DNA-binding, has been crystallized using the hanging drop vapour diffusion method. X-ray studies show that the crystals belong to the trigonal space group P3(1)21 (or P3(2)21) with a = b = 60.4 A, c = 58.8 A and gamma = 120 degrees. The asymmetric unit contains one molecule. The crystals diffract to at least 3 A resolution and are suitable for X-ray structure analysis.

Publication types

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

MeSH terms

Bacterial Outer Membrane Proteins / chemistry*
Crystallization
Crystallography, X-Ray
DNA-Binding Proteins / chemistry*
DNA-Binding Proteins / physiology
Escherichia coli / chemistry*
Escherichia coli / genetics
Gene Expression Regulation, Bacterial / physiology*
Water-Electrolyte Balance / genetics

Substances

Bacterial Outer Membrane Proteins
DNA-Binding Proteins