@article{,
title = {Crystallization of aspartyl-tRNA synthetase-tRNA(Asp) complex from Escherichia coli and first crystallographic results},
author = {S Eiler and M Boeglin and F Martin and G Eriani and J Gangloff and J C Thierry and D Moras},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1569573},
isbn = {1569573},
year = {1992},
date = {1992-01-01},
journal = {J Mol Biol},
volume = {224},
number = {4},
pages = {1171-1173},
abstract = {Crystals of the dimeric aspartyl-tRNA synthetase from Escherichia coli (molecular mass 132,000 Da) complexed with its cognate tRNA (molecular mass 25,000 Da) have been grown using ammonium sulfate as precipitant. The crystals belong to the orthorhombic space group C222(1) with unit cell parameters a = 102.75 A},
note = {0022-2836
Journal Article},
keywords = {Asp/*ultrastructure X-Ray Diffraction, Aspartate-tRNA Ligase/*ultrastructure Crystallography Escherichia coli/enzymology RNA, ERIANI, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Crystals of the dimeric aspartyl-tRNA synthetase from Escherichia coli (molecular mass 132,000 Da) complexed with its cognate tRNA (molecular mass 25,000 Da) have been grown using ammonium sulfate as precipitant. The crystals belong to the orthorhombic space group C222(1) with unit cell parameters a = 102.75 A