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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt 4):368-71. Epub 2006 Mar 10.

Crystallization and preliminary X-ray analysis of the tRNA thiolation enzyme MnmA from Escherichia coli complexed with tRNA(Glu).

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Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan.


MnmA catalyzes a sulfuration reaction to synthesize 2-thiouridine at the wobble positions of tRNA(Glu), tRNA(Gln) and tRNA(Lys) in Escherichia coli. The binary complex of MnmA and tRNA(Glu) was crystallized in two different crystal forms: forms I and II. Cocrystallization of MnmA-tRNA(Glu) with ATP yielded form III crystals. The three crystal forms diffracted to 3.1, 3.4 and 3.4 angstroms resolution, respectively, using synchrotron radiation at SPring-8. These crystals belong to space groups C2, I2(1)2(1)2(1) and C2, with unit-cell parameters a = 225.4, b = 175.8, c = 53.0 angstroms, beta = 101.6 degrees, a = 101.5, b = 108.0, c = 211.2 A and a = 238.1, b = 102.1, c = 108.2 angstroms, beta = 117.0 degrees, respectively. The asymmetric units of these crystals are expected to contain two, one and two MnmA-tRNA(Glu) complexes, respectively.

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