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Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2368-70. Epub 2004 Nov 26.

Crystallization and preliminary X-ray diffraction analysis of bacteriophage varphi12 packaging factor P7.

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  • 1Institute of Biotechnology and Faculty of Biosciences, Viikki Biocenter, PO Box 56, Viikinkaari 5, University of Helsinki, FIN-00014 Helsinki, Finland.


Bacteriophage varphi12 protein P7 is a structural component of the polymerase complex and ensures stable packaging of the genomic RNA. varphi12 P7 has been cloned, purified and crystallized. Crystals belong to space group P3(2)21, with unit-cell parameters a = 75.7, b = 75.7, c = 45.2 A, alpha = 90, beta = 90, gamma = 120 degrees , and diffract beyond 2.0 A. Multiple anomalous dispersion data have been collected from crystals of selenomethionylated P7. Mass spectroscopy showed proteolysis of the crystallized protein and a truncated form, P7DeltaC, gave crystals of similar morphology. Cross-linking experiments implicated the N-terminal domain of P7 as being essential for dimerization.

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