Crystallography Research Today is a free monthly online journal that collates and summarizes the latest research about Crystallography, including details on x-ray crystals, techniques, analyses, structures.

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

Fukunaga R, Yokoyama S

Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.

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 A resolution data set was collected for the N-terminal fragment. The crystal belongs to the tetragonal space group P4(1) or P4(3), with unit-cell parameters a = b = 101.15, c = 124.24 A. For the C-terminal fragment, a SeMet MAD data set was collected to 3.2 A resolution. The crystal belongs to the orthorhombic space group P222(1), with unit-cell parameters a = 124.15, b = 131.91, c = 138.68 A.

Published 1 March 2007 in Acta Crystallograph Sect F Struct Biol Cryst Commun, 63: 224-8.
Full-text of this article is available online (may require subscription).

© 2005-2008 Crystallography Research Today. All Rights Reserved.