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

Dominic Corollo, Merilyn Blair-Johnson, Joel Conrad, Tristan Fiedler, Danhui Sun, Lan Wang, James Ofengand, Roger Fenna

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

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 Å and have two molecules in the crystallographic asymmetric unit. The flash-frozen crystals diffract X-rays to at least 2.3 Å resolution and appear suitable for crystal structure determination.

Original languageEnglish (US)
Pages (from-to)302-304
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number1
DOIs
StatePublished - Jan 1 1999

ASJC Scopus subject areas

  • Structural Biology

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