Abstract
The crystal structure of the dimeric gene V protein of bacteriophage f1 was determined using multiwavelength anomalous diffraction on the selenomethionine-containing wild-type and isoleucine-47 → methionine mutant proteins with x-ray diffraction data phased to 2.5 Å resolution. The structure of the wild-type protein has been refined to an R factor of 19.2% using native data to 1.8 Å resolution. The structure of the gene V protein was used to obtain a model for the protein portion of the gene V protein- single-stranded DNA complex.
Original language | English |
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Pages (from-to) | 2071-2075 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 91 |
Issue number | 6 |
DOIs | |
Publication status | Published - Mar 15 1994 |
Externally published | Yes |
Keywords
- DNA binding protein
- protein structure
- protein-DNA complex
- synchrotron radiation
- x-ray crystallography
ASJC Scopus subject areas
- General