Crystallization and preliminary X-ray analysis of the C/EBPbeta C-terminal region in complex with DNA.
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.
Tahirov
T H
TH
Bio-Crystallography Technology Division, RIKEN Harima Institute/SPring-8, 1-1-1 Kouto, Mikazuki, Sayo, Hyogo 679-5148, Japan. tahir@med.yokohama-cu.ac.jp
Inoue-Bungo
T
T
Sasaki
M
M
Fujikawa
A
A
Kimura
K
K
Sato
K
K
Adachi
S
S
Kamiya
N
N
Ogata
K
K
D022782:CCAAT-Enhancer-Binding Protein-beta / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry*; D017353:Gene Deletion; D006801:Humans; D009690:Nucleic Acid Conformation; D011487:Protein Conformation
D022782:CCAAT-Enhancer-Binding Protein-beta; D004247:DNA