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Cloning, expression, purification, crystallization and preliminary X-ray diffraction data of the Pyrococcus horikoshii RadA intein

  1. Author:
    Lyskowski, A.
    Oeemig, J. S.
    Jaakkonen, A.
    Rommi, K.
    DiMaio, F.
    Zhou, D. W.
    Kajander, T.
    Baker, D.
    Wlodawer, A.
    Goldman, A.
    Iwai, H.

  2. Author Address

    [Lyskowski, A; Oeemig, JS; Jaakkonen, A; Rommi, K; Kajander, T; Goldman, A; Iwai, H] Univ Helsinki, Inst Biotechnol, Res Program Struct Biol & Biophys, FIN-00014 Helsinki, Finland [DiMaio, F; Baker, D] Univ Washington, Dept Biochem, Seattle, WA 98195 USA [Zhou, DW; Wlodawer, A] NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA;Goldman, A (reprint author), Univ Helsinki, Inst Biotechnol, Res Program Struct Biol & Biophys, POB 65, FIN-00014 Helsinki, Finland;adrian.goldman@helsinki.fi hideo.iwai@helsinki.fi
    1. Year: 2011
    2. Date: May
  2. Journal: Acta Crystallographica Section F-Structural Biology and Crystallization Communications
    1. 67
    2. Pages: 623-626
  4. Type of Article: Article
  5. ISSN: 1744-3091
  1. Abstract:

    The RadA intein from the hyperthermophilic archaebacterium Pyrococcus horikoshii was cloned, expressed and purified for subsequent structure determination. The protein crystallized rapidly in several conditions. The best crystals, which diffracted to 1.75 angstrom resolution, were harvested from drops consisting of 0.1 M HEPES pH 7.5, 3.0 M NaCl and were cryoprotected with Paratone-N before flash-cooling. The collected data were processed in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 58.1, b = 67.4, c = 82.9 angstrom. Molecular replacement with Rosetta using energy-and density-guided structure optimization provided the initial solution, which is currently under refinement.

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External Sources

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  2. DOI: 10.1107/s1744309111008372
  3. View record in Web of Science®
  4. WOS: 000290235900023

Library Notes

  1. Fiscal Year: FY2010-2011
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