Expression, purification, crystallization and preliminary diffraction studies of the tRNA pseudouridine synthase TruD from Escherichia coli.
Pseudouridine, the 5-ribosyl isomer of uridine, is the most common modification of structural RNA. The recently identified pseudouridine synthase TruD belongs to a widespread class of pseudouridine synthases without significant sequence homology to previously known families. TruD from Escherichia coli was overexpressed, purified and crystallized. The crystals diffract to a minimum Bragg spacing of 2.4 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 63.4, b = 108.6, c = 111.7 A.
Ericsson
Ulrika B
UB
Department of Biochemistry and Biophysics, Stockholm University, Roslagstullsbacken 15, SE-114 21 Stockholm, Sweden.
Andersson
Martin E
ME
Engvall
Benita
B
Nordlund
Pär
P
Hallberg
B Martin
BM
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006836:Hydro-Lyases / Q000737:chemistry; D019751:Intramolecular Transferases / Q000737:chemistry*
D029968:Escherichia coli Proteins; D006836:Hydro-Lyases; C022479:pseudouridylate synthetase; D019751:Intramolecular Transferases; C487102:TruD protein, E coli; C023199:tRNA-pseudouridine synthase I