Purification, crystallization and initial X-ray analysis of the head-tail connector of bacteriophage phi29.
The head-tail connector of bacteriophage phi29, an oligomer of gene product 10 (gp10), was crystallized into various forms. The most useful of these were an orthorhombic P22(1)2(1) form (unit-cell parameters a = 143.0, b = 157.0, c = 245.2 A), a monoclinic C2 form (a = 160.7, b = 143.6, c = 221.0 A, beta = 97.8 degrees ) and another monoclinic C2 form (a = 177.0, b = 169.1, c = 185.2 A, beta = 114.1 degrees ). Frozen crystals diffracted to about 3.2 A resolution. There is one connector per crystallographic asymmetric unit in each case. Rotation functions show the connector to be a dodecamer. Translation functions readily determined the position of the 12-fold axis in each unit cell. The structure is being determined by 12-fold electron-density averaging within each crystal and by averaging between the various crystal forms.
Badasso
M O
MO
Department of Microbiology and Oral Science, University of Minnesota, Minneapolis, MN 55455, USA.
Leiman
P G
PG
Tao
Y
Y
He
Y
Y
Ohlendorf
D H
DH
Rossmann
M G
MG
Anderson
D
D
D017103:Bacillus Phages / Q000235:genetics; D002213:Capsid / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D036022:Capsid Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015394:Molecular Structure; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification
D036022:Capsid Proteins; D011994:Recombinant Proteins; C097975:portal protein, bacteriophage phi29