The head-tail connector of bacteriophage φ29, an oligomer of gene product 10 (gp10), was crystallized into various forms. The most useful of these were an orthorhombic P22121 form (unit-cell parameters a = 143.0, b = 157.0, c = 245.2 Å), a monoclinic C2 form (a = 160.7, b = 143.6, c = 221.0 Å, β = 97.8°) and another monoclinic C2 form (a = 177.0, b = 169.1, c = 185.2 Å, β = 114.1°). Frozen crystals diffracted to about 3.2 Å 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.
|Original language||English (US)|
|Number of pages||4|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|State||Published - Oct 3 2000|
ASJC Scopus subject areas
- Structural Biology