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Production, crystallization and preliminary X-ray crystallographic studies of the bacteriophage phi 12 packaging motor.
Acta Crystallogr D Biol Crystallogr. 2004 Mar; 60(Pt 3):588-90.AC

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.

Authors+Show Affiliations

Mancini EJ
Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN, England.
Kainov DE
No affiliation info available
Wei H
No affiliation info available
Gottlieb P
No affiliation info available
Tuma R
No affiliation info available
Bamford DH
No affiliation info available
Stuart DI
No affiliation info available
Grimes JM
No affiliation info available

MeSH

Adenosine TriphosphatasesBacteriophagesCapsidCrystallizationCrystallography, X-RayDNAEscherichia coliProtein SubunitsRecombinant ProteinsSelenomethionine

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

14993703

Citation

Mancini, Erika J., et al. "Production, Crystallization and Preliminary X-ray Crystallographic Studies of the Bacteriophage Phi 12 Packaging Motor." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 3, 2004, pp. 588-90.
Mancini EJ, Kainov DE, Wei H, et al. Production, crystallization and preliminary X-ray crystallographic studies of the bacteriophage phi 12 packaging motor. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 3):588-90.
Mancini, E. J., Kainov, D. E., Wei, H., Gottlieb, P., Tuma, R., Bamford, D. H., Stuart, D. I., & Grimes, J. M. (2004). Production, crystallization and preliminary X-ray crystallographic studies of the bacteriophage phi 12 packaging motor. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 3), 588-90.
Mancini EJ, et al. Production, Crystallization and Preliminary X-ray Crystallographic Studies of the Bacteriophage Phi 12 Packaging Motor. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 3):588-90. PubMed PMID: 14993703.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Production, crystallization and preliminary X-ray crystallographic studies of the bacteriophage phi 12 packaging motor. AU - Mancini,Erika J, AU - Kainov,Denis E, AU - Wei,Hui, AU - Gottlieb,Paul, AU - Tuma,Roman, AU - Bamford,Dennis H, AU - Stuart,David I, AU - Grimes,Jonathan M, Y1 - 2004/02/25/ PY - 2003/11/21/received PY - 2004/01/14/accepted PY - 2004/3/3/pubmed PY - 2004/11/13/medline PY - 2004/3/3/entrez SP - 588 EP - 90 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 3 N2 - 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. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/14993703/Production_crystallization_and_preliminary_X_ray_crystallographic_studies_of_the_bacteriophage_phi_12_packaging_motor_ DB - PRIME DP - Unbound Medicine ER -