Open AccessCrystallization and preliminary X‐ray crystallographic study of alanyl‐tRNA synthetase from the archaeon Archaeoglobus fulgidus
Author(s) -
Fukunaga Ryuya,
Yokoyama Shigeyuki
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107006264
Subject(s) - orthorhombic crystal system , crystallography , tetragonal crystal system , crystallization , escherichia coli , transfer rna , chemistry , resolution (logic) , crystal structure , fragment (logic) , domain (mathematical analysis) , biochemistry , gene , rna , organic chemistry , mathematical analysis , mathematics , artificial intelligence , computer science , programming language
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 P 4 1 or P 4 3 , 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 P 222 1 , with unit‐cell parameters a = 124.15, b = 131.91, c = 138.68 Å.