TY - JOUR
T1 - Crystallization and characterization of a fragment of pseudouridine synthase RluC from Escherichia coli
AU - Corollo, Dominic
AU - Blair-Johnson, Merilyn
AU - Conrad, Joel
AU - Fiedler, Tristan
AU - Sun, Danhui
AU - Wang, Lan
AU - Ofengand, James
AU - Fenna, Roger
PY - 1999/1/1
Y1 - 1999/1/1
N2 - 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.
AB - 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.
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U2 - 10.1107/S090744499801021X
DO - 10.1107/S090744499801021X
M3 - Article
C2 - 10089432
AN - SCOPUS:0032897335
VL - 55
SP - 302
EP - 304
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 1
ER -