Crystallization and preliminary X-ray crystallographic studies on the bacteriophage phi6 RNA-dependent RNA polymerase.
The RNA-dependent RNA polymerase (P2) from bacteriophage Phi6 has been cloned and the protein overexpressed in Escherichia coli to produce an active enzyme. A fully substituted selenomethionyl version of the protein has also been produced. Crystals of both proteins have been grown; most belong to the monoclinic space group P2(1), with unit-cell parameters a = 105.9, b = 94.0, c = 140.9 A, beta = 101.4 degrees, but some are trigonal (space group P3(1) or P3(2)), with unit-cell parameters a = b = 110.1, c = 159.4 A, gamma = 120 degrees. Both crystal forms occur in the same crystallization drop and are morphologically indistinguishable. Native data sets have been collected from both types of crystals to better than 3 A resolution.
Butcher
S J
SJ
Department of Biosciences and Institute of Biotechnology, University of Helsinki, PL56 (Viikinkaari 5), FIN-00014 University of Helsinki, Finland.
Makeyev
E V
EV
Grimes
J M
JM
Stuart
D I
DI
Bamford
D H
DH
D017126:Bacteriophage phi 6 / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D012324:RNA-Dependent RNA Polymerase / Q000737:chemistry*
D012324:RNA-Dependent RNA Polymerase