title: Crystallization, X-ray studies, and site-directed cysteine mutagenesis of the DNA-binding domain of OmpR.
abstract: A C-terminal fragment of the transcription factor OmpR has been crystallized using the sitting drop vapor-diffusion method. Crystals belong to the trigonal space-group P3n12 with cell dimensions a = b = 54.4 A, c = 135.5 A, and gamma = 120.00 degrees. A second crystal form has been obtained by soaking this crystal form in a cryo-buffer and flash-cooling to 108 K in a cold nitrogen stream. Crystals belong to the trigonal space-group P3n12 with cell dimensions a = b = 108.07 A, c = 131.81 A, and gamma = 120.00 degrees. Both crystal forms diffract to at least 2.3 A at a synchrotron light source. Single-site cysteine mutations have been introduced to provide mercury-binding sites for multiple isomorphous replacement.
authors.affiliation: Center for Advanced Biotechnology and Medicine, Piscataway, New Jersey 08854, USA.
authors.forename: E
authors.initials: E
authors.lastname: Martínez-Hackert
authors.forename: S
authors.initials: S
authors.lastname: Harlocker
authors.forename: M
authors.initials: M
authors.lastname: Inouye
authors.forename: H M
authors.initials: HM
authors.lastname: Berman
authors.forename: A M
authors.initials: AM
authors.lastname: Stock
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D016415:Sequence Alignment
chemical_list: D001425:Bacterial Outer Membrane Proteins; D004268:DNA-Binding Proteins; D011994:Recombinant Proteins