Abstract
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) |
|---|---|
| Pages (from-to) | 1187-1190 |
| Number of pages | 4 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 56 |
| Issue number | 9 |
| DOIs | |
| State | Published - 2000 |
| Externally published | Yes |
ASJC Scopus subject areas
- Structural Biology
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