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Crystallization of a small fragment of an aminoacyl tRNA synthetase

Academic Article
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Overview

authors

  • Frederick, C. A.
  • Wang, A. H. J.
  • Rich, A.
  • Regan, L.
  • Schimmel, Paul

publication date

  • September 1988

journal

  • Journal of Molecular Biology  Journal

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.

subject areas

  • Alanine-tRNA Ligase
  • Amino Acids
  • Amino Acyl-tRNA Synthetases
  • Crystallization
  • Escherichia coli
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/0022-2836(88)90019-8

PubMed ID

  • 3058989
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Additional Document Info

start page

  • 521

end page

  • 522

volume

  • 203

issue

  • 2

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