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 language||English (US)|
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|State||Published - Jan 1 1999|
ASJC Scopus subject areas
- Structural Biology