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

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|65|6|618-620

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.65, Iss.6, 2009-06, pp. : 618-620

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Abstract

Methionyl‐tRNA synthetase (MetRS) from Mycobacterium smegmatis was recombinantly expressed in Escherichia coli and purified using Ni2+‐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 Å 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 Å, β = 124.8°. The presence of three molecules in the asymmetric unit corresponded to a solvent content of 60% and a Matthews coefficient of 3.1 Å3 Da−1. Structure determination is in progress.