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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.

Original publication

DOI

10.1107/S0907444904001052

Type

Journal article

Journal

Acta Crystallogr D Biol Crystallogr

Publication Date

03/2004

Volume

60

Pages

588 - 590

Keywords

Adenosine Triphosphatases, Bacteriophages, Capsid, Crystallization, Crystallography, X-Ray, DNA, Escherichia coli, Protein Subunits, Recombinant Proteins, Selenomethionine