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 of lithium sulfate was critical for crystal nucleation. Crystals diffracted well beyond a resolution of 1.6 A and were found to belong to the orthorhombic space group C222(1), with unit-cell parameters a = 79.89, b = 230.42, c = 135.60 A. There is one dimer (M(r) approximately 113 kDa) in the asymmetric unit, with a solvent content of 55%. Efforts to solve the phase problem by molecular replacement are under way.
Chimnaronk
Sarin
S
Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8562, Japan.
Jeppesen
Mads Gravers
MG
Shimada
Nobukazu
N
Suzuki
Tsutomu
T
Nyborg
Jens
J
Watanabe
Kimitsuna
K
D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D008928:Mitochondria / Q000201:enzymology* / Q000235:genetics; D009690:Nucleic Acid Conformation; D012714:Serine-tRNA Ligase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D012714:Serine-tRNA Ligase