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Crystallization and preliminary X-ray diffraction studies of NusG, a protein shared by the transcription and translation machines

  1. Author:
    Andrykovitch, M.
    Guo, W.
    Routzahn, K. M.
    Gu, Y. J.
    Anderson, D. E.
    Reshetnikova, L. S.
    Knowlton, J. R.
    Waugh, D. S.
    Ji, X. H.

  2. Author Address

    NCI, Biomol Struct Sect, Macromol Crystallog Lab, NIH, Frederick, MD 21702 USA NCI, Biomol Struct Sect, Macromol Crystallog Lab, NIH, Frederick, MD 21702 USA NCI, Prot Engn Sect, Macromol Crystallog Lab, NIH, Frederick, MD 21702 USA Ji XH NCI, Biomol Struct Sect, Macromol Crystallog Lab, NIH, Frederick, MD 21702 USA
    1. Year: 2002
  2. Journal: Acta Crystallographica Section D-Biological Crystallography
    1. 58
    2. Part 12
    3. Pages: 2157-2158
  4. Type of Article: Article
  1. Abstract:

    N-utilization factor G (NusG) from Aquifex aeolicus (Aa) was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapor-diffusion technique. The drops consisted of 2.5 mul protein solution (similar to30 mg ml(-1) in 20 mM Tris-HCl pH 8.0, 200 mM NaCl, 2 mM EDTA and 10 mM DTT) and 2.5 mul reservoir solution (0.085 M Na HEPES pH 7.5, 15% glycerol, 11% 2-propanol and 20% PEG 4000) derived from condition number 41 of the Hampton Cryo Screen. The crystals grew at 291 +/- 1 K and reached dimensions of 0.2 x 0.1 x 0.05 mm in 5-7 d. The crystals, which diffracted to 2.45 Angstrom resolution, belonged to space group C222(1), with unit-cell parameters a = 65.95, b = 124.58, c = 83.60 Angstrom. One AaNusG molecule is present in the asymmetric unit, corresponding to a solvent content of 59.80% (Matthews coefrcient = 3.06 Angstrom(3) Da(-1)). Crystal structure determination is in progress.

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