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  • Title: Production, crystallization and preliminary X-ray crystallographic studies of the bacteriophage phi 12 packaging motor.
    Author: Mancini EJ, Kainov DE, Wei H, Gottlieb P, Tuma R, Bamford DH, Stuart DI, Grimes JM.
    Journal: Acta Crystallogr D Biol Crystallogr; 2004 Mar; 60(Pt 3):588-90. PubMed ID: 14993703.
    Abstract:
    The hexameric ATPase P4 from bacteriophage phi 12 is responsible for packaging single-stranded genomic precursors into the viral procapsid. P4 was overexpressed in Escherichia coli and purified. Crystals of native and selenomethionine-derivatized P4 have been obtained that belong to space group I222, with half a hexamer in the asymmetric unit and unit-cell parameters a = 105.0, b = 130.5, c = 158.9 A. A second crystal form of different morphology can occur in the same crystallization drop. The second form belongs to space group P1, with four hexamers in the asymmetric unit and unit-cell parameters a = 114.9, b = 125.6, c = 153.9 A, alpha = 90.1, beta = 91.6, gamma = 90.4 degrees. Synchrotron X-ray diffraction data have been collected for the I222 and P1 crystal forms to 2.0 and 2.5 A resolution, respectively.
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