Characterization of the chymotryptic core of the adenovirus DNA‐binding protein
- 2 September 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 188 (2) , 248-252
- https://doi.org/10.1016/0014-5793(85)80381-1
Abstract
A fragment of the DNA‐binding protein of adenovirus type 5 has been obtained by controlled chymotryptic digestion of the entire molecule. Partial sequence determination indicates that the fragment consists of amino acids 174–525. The fragment is biologically active as measured by its ability to substitute for the entire molecule in a reconstituted DNA replication system. Crystals have been obtained that show diffraction to 2 Å.Keywords
This publication has 35 references indexed in Scilit:
- Detection of a bromoperoxidase inStreptomyces phaeochromogenesFEBS Letters, 1984
- Novel crystal forms of a proteolytic core of the single‐stranded DNA‐binding protein (SSB) from E. coliFEBS Letters, 1984
- Crystallization of a fragment of the adenovirus DNA binding proteinJournal of Molecular Biology, 1984
- Crystals of Escherichia coli single-strand DNA-binding protein show that the tetramer has D2 symmetryJournal of Molecular Biology, 1983
- Structural analysis of T4 DNA helix destabilizing protein (gp32*I) crystal by electron microscopyJournal of Molecular Biology, 1983
- Crystallization of a tryptic core of the single-stranded DNA binding protein of bacteriophage T4Journal of Molecular Biology, 1982
- Partial proteolysis of the natural ATPase inhibitor from beef heart mitochondriaFEBS Letters, 1981
- Interaction between the adenovirus DNA-binding protein and double-stranded DNAJournal of Molecular Biology, 1979
- Mutations that allow human Ad2 and Ad5 to express late genes in monkey cells map in the viral gene encoding the 72K DNA binding proteinCell, 1979
- Complex Formation between the Adenovirus Type 5 DNA‐Binding Protein and Single‐Stranded DNAEuropean Journal of Biochemistry, 1978