Crystallization and preliminary X-ray diffraction study of mammalian mitochondrial seryl-tRNA synthetase

The mitochondrial seryl‐tRNA synthetase (mt SerRS) from Bos taurus was overexpressed in Escherichia coli and crystallized using the sitting‐drop vapour‐diffusion method. Crystals grew in a very narrow range of conditions using PEG 8000 as precipitant at room temperature. An appropriate concentration...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2004-07, Vol.60 (7), p.1319-1322
Main Authors: Chimnaronk, Sarin, Jeppesen, Mads Gravers, Shimada, Nobukazu, Suzuki, Tsutomu, Nyborg, Jens, Watanabe, Kimitsuna
Format: Article
Language:English
Subjects:
Animals
Base Sequence
Bos taurus
Cattle
Crystallization
Crystallography, X-Ray
Gene Expression
mitochondria
Mitochondria - enzymology
Mitochondria - genetics
Nucleic Acid Conformation
Serine-tRNA Ligase - chemistry
Serine-tRNA Ligase - genetics
Serine-tRNA Ligase - isolation & purification
seryl-tRNA synthetase
translation
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Summary:The mitochondrial seryl‐tRNA synthetase (mt SerRS) from Bos taurus was overexpressed in Escherichia coli and crystallized using the sitting‐drop vapour‐diffusion method. Crystals grew in a very narrow range of conditions using PEG 8000 as precipitant at room temperature. An appropriate concentration of lithium sulfate was critical for crystal nucleation. Crystals diffracted well beyond a resolution of 1.6 Å and were found to belong to the orthorhombic space group C2221, with unit‐cell parameters a = 79.89, b = 230.42, c = 135.60 Å. There is one dimer (Mr≃ 113 kDa) in the asymmetric unit, with a solvent content of 55%. Efforts to solve the phase problem by molecular replacement are under way.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444904011217