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. 1997 Jul 1;25(13):2620-6.
doi: 10.1093/nar/25.13.2620.

Characterization and crystallization of the helicase domain of bacteriophage T7 gene 4 protein

L E Bird  1 , K Hâkansson, H Pan, D B Wigley
Affiliations

Characterization and crystallization of the helicase domain of bacteriophage T7 gene 4 protein

L E Bird et al. Nucleic Acids Res. .

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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References

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