PMID:10089432
| Citation |
Corollo, D, Blair-Johnson, M, Conrad, J, Fiedler, T, Sun, D, Wang, L, Ofengand, J and Fenna, R (1999) Crystallization and characterization of a fragment of pseudouridine synthase RluC from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 55:302-4 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1107/S090744499801021X |
| Keywords |
Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression; Hydro-Lyases/chemistry; Hydro-Lyases/genetics; Hydro-Lyases/isolation & purification; Peptide Fragments/chemistry; Peptide Fragments/genetics; Peptide Fragments/isolation & purification; RNA, Bacterial; RNA, Ribosomal, 23S; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification |
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