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.
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.
Kondo
H
H
Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan.
Miyaji
T
T
Suzuki
M
M
Tate
S
S
Mizuno
T
T
Nishimura
Y
Y
Tanaka
I
I
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000502:physiology; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D014882:Water-Electrolyte Balance / Q000235:genetics
D001425:Bacterial Outer Membrane Proteins; D004268:DNA-Binding Proteins