Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 3 (March 2007)

crystallization communications

Acta Cryst. (2007). F63, 224-228 [ doi:10.1107/S1744309107006264 ]

Crystallization and preliminary X-ray crystallographic study of alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidus

R. Fukunaga and S. Yokoyama

Abstract: In order to analyze the alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidus, the N-terminal fragment lacking the dimerization domain and the C-terminal dimerization-domain fragment were each overexpressed in Escherichia coli, purified and crystallized. A 3.7 Å resolution data set was collected for the N-terminal fragment. The crystal belongs to the tetragonal space group P4₁ or P4₃, with unit-cell parameters a = b = 101.15, c = 124.24 Å. For the C-terminal fragment, a SeMet MAD data set was collected to 3.2 Å resolution. The crystal belongs to the orthorhombic space group P222₁, with unit-cell parameters a = 124.15, b = 131.91, c = 138.68 Å.

Keywords: AlaRS; tRNa; alanine; editing; dimerization; Archaeoglobus fulgidus.