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

• DOI: 10.1073/pnas.91.6.2071
• Publication Date: 2006-05-31T13:05:57Z
• Authors: M M Skinner; H Zhang; D H Leschnitzer; Y Guan; H Bellamy; R M Sweet; C W Gray; R N Konings; A H Wang; T C Terwilliger
• Keywords: Models, Molecular; Viral Proteins; 0303 health sciences; 03 medical and health sciences; Inovirus; Crystallography, X-Ray; Selenomethionine

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.