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Crystallization of Mycobacterium smegmatis methionyl-tRNA synthetase in the presence of methionine and adenosine.

Authors
  • Ingvarsson, Henrik
  • Jones, T Alwyn
  • Unge, Torsten
Type
Published Article
Journal
Acta Crystallographica Section F Structural Biology and Crystallization Communications
Publisher
International Union of Crystallography
Publication Date
Jun 01, 2009
Volume
65
Issue
Pt 6
Pages
618–620
Identifiers
DOI: 10.1107/S1744309109016704
PMID: 19478446
Source
Medline
License
Unknown

Abstract

Methionyl-tRNA synthetase (MetRS) from Mycobacterium smegmatis was recombinantly expressed in Escherichia coli and purified using Ni(2+)-affinity and size-exclusion chromatography. Crystals formed readily in the presence of the ligands methionine and adenosine. These two ligands are components of an intermediate in the two-step catalytic mechanism of MetRS. The crystals were produced using the vapour-diffusion method and a full data set to 2.1 A resolution was collected from a single crystal. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 155.9, b = 138.9, c = 123.3 A, beta = 124.8 degrees . The presence of three molecules in the asymmetric unit corresponded to a solvent content of 60% and a Matthews coefficient of 3.1 A(3) Da(-1). Structure determination is in progress.

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