Crystallization and preliminary X-ray analysis of the Tet-repressor/operator complex.
Three crystal forms of the repressor protein TetR class D in complex with the palindromic 17 bp operator sequence containing T overhangs on both sides were obtained by hanging-drop vapor-diffusion methods using PEG 4000 and PEG monomethylether 5000 as precipitants. Although the crystallization conditions were very similar, up to three different crystal forms were observed in the same drop. The space groups are monoclinic C2, P21 and hexagonal P6122. The asymmetric units of the latter two crystal forms contain one repressor-operator complex. The crystal structures of these forms were solved by molecular replacement using the Tet-repressor molecule of the complex with tetracycline as a search model.
Orth
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P
Institut für Kristallographie, Freie Universität Berlin, Takustrasse 6, D-14195 Berlin, Germany.
Alings
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C
Schnappinger
D
D
Saenger
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Hinrichs
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W
D001483:Base Sequence; D003460:Crystallization; D008969:Molecular Sequence Data; D009875:Operator Regions, Genetic; D012097:Repressor Proteins / Q000737:chemistry*; D012689:Sequence Homology, Nucleic Acid; D014961:X-Ray Diffraction
D012097:Repressor Proteins; C034811:tetracycline resistance-encoding transposon repressor protein