Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 1 (January 2007)

crystallization communications

Acta Cryst. (2007). F63, 46-48 [ doi:10.1107/S1744309106052870 ]

Crystallization and preliminary X-ray diffraction analysis of an Escherichia coli tRNA^Gly acceptor-stem microhelix

C. Förster, M. Perbandt, A. B. E. Brauer, S. Brode, J. P. Fürste, C. Betzel and V. A. Erdmann

Abstract: The tRNA^Gly and glycyl-tRNA synthetase (GlyRS) system is an evolutionary special case within the class II aminoacyl-tRNA synthetases because two divergent types of GlyRS exist: an archaebacterial/human type and an eubacterial type. The tRNA identity elements which determine the correct aminoacylation process are located in the aminoacyl domain of tRNA^Gly. To obtain further insight concerning structural investigation of the identity elements, the Escherichia coli seven-base-pair tRNA^Gly acceptor-stem helix was crystallized. Data were collected to 2.0 Å resolution using synchrotron radiation. Crystals belong to space group P3₁21 or P3₂21, with unit-cell parameters a = b = 35.35, c = 130.82 Å, [alpha] = [beta] = 90, [gamma] = 120° and two molecules in the asymmetric unit.

Keywords: tRNA acceptor-stem microhelix; tRNA identity elements; tRNA^Gly; glycyl-tRNA synthetase; class II aminoacyl-tRNA synthetases.