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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1994 Mar 15;91(6):2071–2075. doi: 10.1073/pnas.91.6.2071

Structure of the gene V protein of bacteriophage f1 determined by multiwavelength x-ray diffraction on the selenomethionyl protein.

M M Skinner 1, H Zhang 1, D H Leschnitzer 1, Y Guan 1, H Bellamy 1, R M Sweet 1, C W Gray 1, R N Konings 1, A H Wang 1, T C Terwilliger 1
PMCID: PMC43311  PMID: 8134350

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 A resolution. The structure of the wild-type protein has been refined to an R factor of 19.2% using native data to 1.8 A 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.

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Selected References

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