Crystallization, X-ray studies, and site-directed cysteine mutagenesis of the DNA-binding domain of OmpR.
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.
Martínez-Hackert
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E
Center for Advanced Biotechnology and Medicine, Piscataway, New Jersey 08854, USA.
Harlocker
S
S
Inouye
M
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Berman
H M
HM
Stock
A M
AM
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
D001425:Bacterial Outer Membrane Proteins; D004268:DNA-Binding Proteins; D011994:Recombinant Proteins