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- W2014676187 abstract "The seryl-tRNA synthetase (SerRS) from Candida albicans exists naturally as two isoforms resulting from ambiguity in the natural genetic code. Both enzymes were crystallized by the sitting-drop vapour-diffusion method using 3.2–3.4 M ammonium sulfate as precipitant. The crystals belonged to the hexagonal space group P6122 and contained one monomer per asymmetric unit, despite the synthetase existing as a homodimer (with a molecular weight of ∼116 kDa) in solution. Diffraction data were collected to 2.0 Å resolution at a synchrotron source and the crystal structures of unliganded SerRS and of its complexes with ATP and with a seryl-adenylate analogue were solved by molecular replacement. The structure of C. albicans SerRS represents the first reported structure of a eukaryotic cytoplasmic SerRS." @default.
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- W2014676187 date "2010-12-24" @default.
- W2014676187 modified "2023-09-27" @default.
- W2014676187 title "Purification, crystallization and preliminary X-ray diffraction analysis of the seryl-tRNA synthetase from<i>Candida albicans</i>" @default.
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- W2014676187 doi "https://doi.org/10.1107/s1744309110048542" @default.
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