Crystallization and initial X-ray diffraction studies of scaffolding protein (gp7) of bacteriophage phi29.
The Bacillus subtilis bacteriophage phi29 scaffolding protein (gp7) has been crystallized by the hanging-drop vapour-diffusion method at 293 K. Two new distinct crystal forms that both differed from a previously crystallized and solved scaffolding protein were grown under the same conditions. Form I belongs to the primitive tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 77.13, c = 37.12 A. Form II crystals exhibit an orthorhombic crystal form, with space group C222 and unit-cell parameters a = 107.50, b = 107. 80, c = 37.34 A. Complete data sets have been collected to 1.78 and 1.80 A for forms I and II, respectively, at 100 K using Cu Kalpha X-rays from a rotating-anode generator. Calculation of a VM value of 2.46 A3 Da(-1) for form I suggests the presence of one molecule in the asymmetric unit, corresponding to a solvent content of 50.90%, whereas form II has a VM of 4.80 A3 Da(-1) with a solvent content of 48.76% and two molecules in the asymmetric unit. The structures of both crystal forms are being determined by the molecular-replacement method using the coordinates of the published crystal structure of gp7.
Badasso
Mohammed O
MO
Department of Oral Science, University of Minnesota, Minneapolis, MN 55455, USA. badas001@umn.edu
Anderson
Dwight L
DL
D017103:Bacillus Phages / Q000737:chemistry*; D003460:Crystallization / Q000379:methods; D015678:Viral Structural Proteins / Q000737:chemistry*; D014835:Volatilization; D014961:X-Ray Diffraction
D015678:Viral Structural Proteins