Crystallization and preliminary X-ray analysis of a proteinase-K-resistant domain within the phosphoprotein of vesicular stomatitis virus (Indiana).
Several stable domains of the phosphoprotein (P) of vesicular stomatitis virus (Indiana) were identified by limited proteolysis of purified recombinant P protein expressed in Escherichia coli. The proteinase-K-resistant domain could be crystallized using ammonium sulfate as a precipitant and ethylene glycol as an additive. The crystals belong to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 74.50, c = 156.84 A. X-ray diffraction data were collected to 2.75 A resolution at a synchrotron-radiation source.
Ding
Haitao
H
Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
Green
Todd J
TJ
Luo
Ming
M
D003460:Crystallization; D018360:Crystallography, X-Ray; D019286:Endopeptidase K / Q000378:metabolism*; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014721:Vesicular stomatitis Indiana virus / Q000737:chemistry* / Q000235:genetics
D010750:Phosphoproteins; D019286:Endopeptidase K