CHARACTERIZATION AND CRYSTALLIZATION OF THE HELICASE DOMAIN OF BACTERIOPHAGE-T7 GENE-4 PROTEIN

Authors
BIRD LE HAKANSSON K PAN H WIGLEY DB
Citation
Le. Bird et al., CHARACTERIZATION AND CRYSTALLIZATION OF THE HELICASE DOMAIN OF BACTERIOPHAGE-T7 GENE-4 PROTEIN, Nucleic acids research, 25(13), 1997, pp. 2620-2626
Citations number
43
Categorie Soggetti
Biology
Journal title
Nucleic acids research → ACNP
ISSN journal
03051048
Volume
25
Issue
13
Year of publication
1997
Pages
2620 - 2626
Database
ISI
SICI code
0305-1048(1997)25:13<2620:CACOTH>2.0.ZU;2-9
Abstract
Limited proteolysis of bacteriophage T7 primase/helicase with endoprot einase Glu-C produces several proteolytic fragments. One of these frag ments, 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 bee n obtained that are suitable for X-ray diffraction studies.