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 P3121 (or P3221) with a = b = 60·4 å, c = 58·8 å and γ = 120°. The asymmetric unit contains one molecule. The crystals diffract to at least 3 å resolution and are suitable for X-ray structure analysis. © 1994 Academic Press Limited.