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Nucleic Acids Res. Jul 1, 1997; 25(13): 2620–2626.
PMCID: PMC146783
Characterization and crystallization of the helicase domain of bacteriophage T7 gene 4 protein.
L E Bird, K Hâkansson, H Pan, and D B Wigley
Laboratory of Molecular Biophysics, Rex Richards Building, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Abstract
Limited proteolysis of bacteriophage T7 primase/helicase with endoproteinase Glu-C produces several proteolytic fragments. One of these fragments, which is derived from the C-terminal region of the protein, was prepared and shown to retain helicase activity. This result supports a model in which the gene 4 proteins consist of functionally separable domains. Crystals of this C-terminal fragment of the protein have been obtained that are suitable for X-ray diffraction studies.
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