Structure of the gene V protein of bacteriophage f1 determined by multiwavelength x-ray diffraction on the selenomethionyl protein.
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.
Skinner
M M
MM
Life Sciences Division, Los Alamos National Laboratory, NM 87545.
Zhang
H
H
Leschnitzer
D H
DH
Guan
Y
Y
Bellamy
H
H
Sweet
R M
RM
Gray
C W
CW
Konings
R N
RN
Wang
A H
AH
Terwilliger
T C
TC
D018360:Crystallography, X-Ray; D017912:Inovirus / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D012645:Selenomethionine / Q000737:chemistry; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics
D014764:Viral Proteins; C069558:gene V protein, Enterobacteria phage f1; D012645:Selenomethionine