Abstract
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 A resolution using synchrotron radiation (lambda = 0.976 A). Crystals belong to space group C2, with unit-cell parameters a = 94.2, b = 26.5, c = 98.1 A, beta = 103.9 degrees.
MeSH terms
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Crystallization / methods
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Crystallography, X-Ray
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DNA-Binding Proteins / biosynthesis*
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / isolation & purification
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Escherichia coli / metabolism
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Herpesvirus 4, Human / chemistry*
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Immediate-Early Proteins / chemistry
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Immediate-Early Proteins / isolation & purification
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Peptide Fragments / chemistry
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Protein Structure, Quaternary
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Trans-Activators / biosynthesis*
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Trans-Activators / chemistry
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Trans-Activators / isolation & purification
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Viral Proteins / biosynthesis*
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Viral Proteins / chemistry
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Viral Proteins / isolation & purification
Substances
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BZLF1 protein, Herpesvirus 4, Human
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DNA-Binding Proteins
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Immediate-Early Proteins
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Peptide Fragments
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Trans-Activators
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Viral Proteins