Production, crystallization and preliminary X-ray crystallographic studies of the bacteriophage phi 12 packaging motor.
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.
Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN, England.
Erika J
EJ
Mancini
Denis E
DE
Kainov
Hui
H
Wei
Paul
P
Gottlieb
Roman
R
Tuma
Dennis H
DH
Bamford
David I
DI
Stuart
Jonathan M
JM
Grimes
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D001435:Bacteriophages / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D002213:Capsid / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D012645:Selenomethionine / Q000737:chemistry
D021122:Protein Subunits; D011994:Recombinant Proteins; D004247:DNA; D012645:Selenomethionine; D000251:Adenosine Triphosphatases