Crystallization and preliminary studies of the DNA-binding domain Za from ADAR1 complexed to left-handed DNA.
The proteolytically defined Z-DNA binding domain Za of human adenosine deaminase type 1 (hADAR1) has been crystallized in complex with the DNA oligomer d(TCGCGCG). The crystals were obtained from a solution containing ammonium sulfate as precipitating agent and belong to the tetragonal space group P4212. A complete diffraction data set has been collected to a resolution of 2.4 A. The unit-cell dimensions are a = b = 85.9, c = 71.3 A. A Raman spectrum of the complex indicates that the DNA in the complex adopts the left-handed Z conformation.
Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
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Schwartz
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Shafer
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Lowenhaupt
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Hanlon
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Herbert
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Rich
D000243:Adenosine Deaminase / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry*; D006801:Humans; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman
D004268:DNA-Binding Proteins; D004247:DNA; D000243:Adenosine Deaminase