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Bacteriophage φ12 protein P7 is a structural component of the polymerase complex and ensures stable packaging of the genomic RNA. φ12 P7 has been cloned, purified and crystallized. Crystals belong to space group P3221, with unit-cell parameters a = 75.7, b = 75.7, c = 45.2 Å, α = 90, β = 90, γ = 120°, and diffract beyond 2.0 Å. Multiple anomalous dispersion data have been collected from crystals of selenomethionylated P7. Mass spectroscopy showed proteolysis of the crystallized protein and a truncated form, P7ΔC, gave crystals of similar morphology. Cross-linking experiments implicated the N-­terminal domain of P7 as being essential for dimerization.

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