"Crystallization and characterization of a fragment of pseudouridine synthase RluC from Escherichia coli."

Corollo D, Blair-Johnson M, Conrad J, Fiedler T, Sun D, Wang L, Ofengand J, Fenna R



Published 1999-02-01 in Acta Crystallogr D Biol Crystallogr volume 55 .

Pubmed ID: 10089432
DOI identifier: -

Abstract:
RluC from E. coli is the enzyme responsible for catalyzing the isomerization of uridines 955, 2504 and 2580 in 23S rRNA to pseudouridine. Histidine-tagged RluC was cloned, overexpressed and purified by nickel-affinity chromatography. A proteolytically derived fragment of the enzyme consisting of residues 89-319 has been shown to retain catalytic activity. Crystals of this fragment, grown by precipitation with sodium acetate at pH 8.0, belong to space group P321, with unit-cell dimensions a = b = 97.1, c = 86.3 A and have two molecules in the crystallographic asymmetric unit. The flash-frozen crystals diffract X-rays to at least 2.3 A resolution and appear suitable for crystal structure determination.


This publication refers to following proteins:



Last modification of this entry: Sept. 6, 2012