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 condi...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1998-01, Vol.54 (1), p.99-100
Main Authors: Orth, Peter, Alings, Claudia, Schnappinger, Dirk, Saenger, Wolfram, Hinrichs, Winfried
Format: Article
Language:English
Subjects:
Base Sequence
Crystallization
Molecular Sequence Data
Operator Regions, Genetic
Repressor Proteins - chemistry
Sequence Homology, Nucleic Acid
X-Ray Diffraction
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Summary: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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444997007646