Purification, crystallization and initial X-ray analysis of the head-tail connector of bacteriophage φ29

M. O. Badasso, P. G. Leiman, Y. Tao, Y. He, D. H. Ohlendorf, M. G. Rossmann, D. Anderson

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

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 languageEnglish (US)
Pages (from-to)1187-1190
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number9
DOIs
StatePublished - 2000
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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