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

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.

Jones, T AlwynUppsala universitet,Strukturell molekylärbiologi(Swepub:uu)alwyjone (författare)
Unge, TorstenUppsala universitet,Strukturell molekylärbiologi(Swepub:uu)torsunge (författare)
Uppsala universitetStrukturell molekylärbiologi (creator_code:org_t)

Ingår i:Acta Crystallographica. Section F65:Part 6, s. 618-6201744-30911744-3091

Av författaren/redakt...: Ingvarsson, Henr ...; Jones, T Alwyn; Unge, Torsten

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