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Title: Expression, purification, crystallization and preliminary X-ray analysis of a C-terminal fragment of the Epstein–Barr virus ZEBRA protein

Abstract

A C-terminal fragment of the Epstein–Barr virus lytic switch protein ZEBRA has been crystallized in complex with DNA. 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 C2, with unit-cell parameters a = 94.2, b = 26.5, c = 98.1 Å, β = 103.9°.

Authors:
 [1];  [2];  [1];  [3]; ;  [1]
  1. European Molecular Biology Laboratory, Grenoble Outstation, BP 181, 38042 Grenoble CEDEX 9 (France)
  2. (France)
  3. Laboratoire de Virologie Moléculaire et Structurale, EA 2939, Université Joseph Fourier, Grenoble (France)
Publication Date:
OSTI Identifier:
22356290
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 3; Other Information: PMCID: PMC2197177; PMID: 16511303; PUBLISHER-ID: fw5065; OAI: oai:pubmedcentral.nih.gov:2197177; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ACETATES; CRYSTALLIZATION; CRYSTALS; DIFFUSION; DIMERS; DNA; ESCHERICHIA COLI; MAGNESIUM; MATHEMATICAL SOLUTIONS; RESOLUTION; SOLUTIONS; SPACE GROUPS; SYNCHROTRON RADIATION

Citation Formats

Morand, Patrice, Laboratoire de Virologie Moléculaire et Structurale, EA 2939, Université Joseph Fourier, Grenoble, Budayova-Spano, Monika, Perrissin, Monique, Müller, Christoph W., E-mail: mueller@embl-grenoble.fr, and Petosa, Carlo. Expression, purification, crystallization and preliminary X-ray analysis of a C-terminal fragment of the Epstein–Barr virus ZEBRA protein. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106002971.
Morand, Patrice, Laboratoire de Virologie Moléculaire et Structurale, EA 2939, Université Joseph Fourier, Grenoble, Budayova-Spano, Monika, Perrissin, Monique, Müller, Christoph W., E-mail: mueller@embl-grenoble.fr, & Petosa, Carlo. Expression, purification, crystallization and preliminary X-ray analysis of a C-terminal fragment of the Epstein–Barr virus ZEBRA protein. United Kingdom. doi:10.1107/S1744309106002971.
Morand, Patrice, Laboratoire de Virologie Moléculaire et Structurale, EA 2939, Université Joseph Fourier, Grenoble, Budayova-Spano, Monika, Perrissin, Monique, Müller, Christoph W., E-mail: mueller@embl-grenoble.fr, and Petosa, Carlo. Wed . "Expression, purification, crystallization and preliminary X-ray analysis of a C-terminal fragment of the Epstein–Barr virus ZEBRA protein". United Kingdom. doi:10.1107/S1744309106002971.
@article{osti_22356290,
title = {Expression, purification, crystallization and preliminary X-ray analysis of a C-terminal fragment of the Epstein–Barr virus ZEBRA protein},
author = {Morand, Patrice and Laboratoire de Virologie Moléculaire et Structurale, EA 2939, Université Joseph Fourier, Grenoble and Budayova-Spano, Monika and Perrissin, Monique and Müller, Christoph W., E-mail: mueller@embl-grenoble.fr and Petosa, Carlo},
abstractNote = {A C-terminal fragment of the Epstein–Barr virus lytic switch protein ZEBRA has been crystallized in complex with DNA. 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 C2, with unit-cell parameters a = 94.2, b = 26.5, c = 98.1 Å, β = 103.9°.},
doi = {10.1107/S1744309106002971},
journal = {Acta Crystallographica. Section F},
number = Pt 3,
volume = 62,
place = {United Kingdom},
year = {Wed Mar 01 00:00:00 EST 2006},
month = {Wed Mar 01 00:00:00 EST 2006}
}