Crystallization and preliminary X-ray analysis of the C/EBPbeta C-terminal region in complex with DNA
| Autor: | Shin-ichi Adachi, Atsushi Fujikawa, Nobuo Kamiya, Kazumi Kimura, Ko Sato, Kazuhiro Ogata, Motoko Sasaki, Tahir H. Tahirov, Taiko Inoue-Bungo |
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| Rok vydání: | 2000 |
| Předmět: |
Leucine zipper
Truncation Fragment (computer graphics) Protein Conformation CCAAT-Enhancer-Binding Protein-beta Resolution (electron density) General Medicine DNA Biology Crystallography X-Ray law.invention Crystallography chemistry.chemical_compound chemistry Structural Biology law Domain (ring theory) Humans Nucleic Acid Conformation Crystallization X ray analysis Gene Deletion |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 57(Pt 6) |
| ISSN: | 0907-4449 |
| Popis: | The C-terminal fragment (residues 259-345) of human C/EBPbeta, a basic region leucine zipper transcriptional regulatory factor which includes the minimal DNA-binding domain, was crystallized in complex with a 16 bp DNA fragment from the tom-1 promoter. The crystals were in the form of a parallelepiped belonging to space group C222(1), had unit-cell parameters a = 100.7 (2), b = 113.5 (1), c = 74.4 (1) A and diffracted to a resolution of 2.1 A. Moreover, truncation of nine residues from the C-terminus not conserved among C/EBP family members yielded isomorphous crystals that diffracted to a resolution of 1.8 A or better. Truncation of 14 residues from the N-terminus of the C-terminal fragment produced well shaped crystals in the form of hexagonal bipyramids, however; unfortunately, they were unstable and diffracted poorly. |
| Databáze: | OpenAIRE |
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