title: Crystallization of a small fragment of an aminoacyl tRNA synthetase.
abstract: Single crystals of an amino-terminal fragment of Escherichia coli alanine tRNA synthetase have been prepared by the vapor diffusion method. The fragment extends to amino acid residue 368 and catalyzes the synthesis of alanyl adenylate. The crystals grow in the presence of alanine as rhombic plates in space group P2(1)2(1)2(1) and with unit cell dimensions of a = 67.9 A, b = 98.5 A and c = 123.6 A (1 A = 0.1 nm). They diffract to better than 3 A resolution.
authors.affiliation: Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
authors.forename: C A
authors.initials: CA
authors.lastname: Frederick
authors.forename: A H
authors.initials: AH
authors.lastname: Wang
authors.forename: A
authors.initials: A
authors.lastname: Rich
authors.forename: L
authors.initials: L
authors.lastname: Regan
authors.forename: P
authors.initials: P
authors.lastname: Schimmel
mesh_terms: D000412:Alanine-tRNA Ligase; D000596:Amino Acids; D000604:Amino Acyl-tRNA Synthetases; D003460:Crystallization; D004926:Escherichia coli
chemical_list: D000596:Amino Acids; D000604:Amino Acyl-tRNA Synthetases; D000412:Alanine-tRNA Ligase