Crystallization and preliminary X-ray analysis of the C/EBPβ C-terminal region in complex with DNA

T. H. Tahirov, T. Inoue-Bungo, M. Sasaki, A. Fujikawa, K. Kimura, K. Sato, S. I. Adachi, N. Kamiya, K. Ogata

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Abstract

The C-terminal fragment (residues 259-345) of human C/EBPβ, 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 C2221, had unit-cell parameters a = 100.7 (2), b = 113.5 (1), c = 74.4 (1) Å and diffracted to a resolution of 2.1 Å. 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 Å 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.

Original languageEnglish (US)
Pages (from-to)854-856
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number6
DOIs
Publication statusPublished - Jul 4 2001

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ASJC Scopus subject areas

  • Structural Biology

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