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.
|頁（從 - 到）||2071-2075|
|期刊||Proceedings of the National Academy of Sciences of the United States of America|
|出版狀態||已發佈 - 3月 15 1994|
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