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Crystallization, X‐ray studies, and site‐directed cysteine mutagenesis of the DNA‐binding domain of OmpR
Author(s) -
MartinezHackert Erik,
Berman Helen M.,
Harlocker Susan,
Inouye Masayori,
Stock Ann M.
Publication year - 1996
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560050722
Subject(s) - crystallography , chemistry , crystallization , cysteine , x ray crystallography , crystal (programming language) , stereochemistry , diffraction , biochemistry , physics , enzyme , optics , programming language , organic chemistry , computer science
A C‐terminal fragment of the transcription factor OmpR has been crystallized using the sitting drop vapor‐diffusion method. Crystals belong to the trigonal spacegroup P3 n 12 with cell dimensions a = b = 54.4 Å, c = 135.5 Å, and γ = 120.00°. 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 P3 n 12 with cell dimensions a = b = 108.07 Å, c = 131.81Å, and γ = 120.00°. Both crystal forms diffract to at least 2.3 Å at a synchrotron light source. Single‐site cysteine mutations have been introduced to provide mercury‐binding sites for multiple isomorphous replacement.