Crystallization and preliminary X-ray crystallographic studies on the bacteriophage phi6 RNA-dependent RNA polymerase

S J Butcher; E V Makeyev; J M Grimes; D I Stuart; D H Bamford

doi:10.1107/s0907444900010702

Crystallization and preliminary X-ray crystallographic studies on the bacteriophage phi6 RNA-dependent RNA polymerase

Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1473-5. doi: 10.1107/s0907444900010702.

Authors

S J Butcher¹, E V Makeyev, J M Grimes, D I Stuart, D H Bamford

Affiliation

¹ Department of Biosciences and Institute of Biotechnology, University of Helsinki, PL56 (Viikinkaari 5), FIN-00014 University of Helsinki, Finland.

PMID: 11053857
DOI: 10.1107/s0907444900010702

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacteriophage phi 6 / enzymology*
Crystallization
Crystallography, X-Ray
Protein Conformation
RNA-Dependent RNA Polymerase / chemistry*

Substances

RNA-Dependent RNA Polymerase