Open AccessExpression, purification, crystallization and preliminary X‐ray analysis of a C‐terminal fragment of the Epstein–Barr virus ZEBRA protein
Author(s) -
Morand Patrice,
BudayovaSpano Monika,
Perrissin Monique,
Müller Christoph W.,
Petosa Carlo
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106002971
Subject(s) - crystallization , leucine zipper , crystallography , recombinant dna , escherichia coli , dimer , protein crystallization , chemistry , microbiology and biotechnology , polyethylene glycol , biology , transcription factor , biochemistry , gene , organic chemistry
A C‐terminal fragment of the Epstein–Barr virus immediate‐early transcription factor ZEBRA has been expressed as a recombinant protein in Escherichia coli and purified to homogeneity. The fragment behaves as a dimer in solution, consistent with the presence of a basic region leucine‐zipper (bZIP) domain. Crystals of the fragment in complex with a DNA duplex were grown by the hanging‐drop vapour‐diffusion technique using polyethylene glycol 4000 and magnesium acetate as crystallization agents. Crystals diffract to better than 2.5 Å resolution using synchrotron radiation (λ = 0.976 Å). Crystals belong to space group C 2, with unit‐cell parameters a = 94.2, b = 26.5, c = 98.1 Å, β = 103.9°.