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Effects of crystal twinning on the ability to solve a macromolecular structure using multiwavelength anomalous diffraction

  1. Author:
    Yang, F.
    Dauter, Z.
    Wlodawer, A.

  2. Author Address

    Wlodawer A NCI, Prot Struct Sec, Macromol Crystallog Lab, Program Struct Biol,FCRDC Frederick, MD 21702 USA NCI, Prot Struct Sec, Macromol Crystallog Lab, Program Struct Biol,FCRDC Frederick, MD 21702 USA Brookhaven Natl Lab, NSLS Upton, NY 11973 USA NCI, Synchrotron Radiat Res Sect, Macromol Crystallog Lab, Program Struct Biol Upton, NY 11973 USA
    1. Year: 2000
  2. Journal: Acta Crystallographica Section D-Biological Crystallography
    1. 56
    2. Part 8
    3. Pages: 959-964
  4. Type of Article: Article
  1. Abstract:

    The crystal structure of gpD, the capsid-stabilizing protein of bacteriophage lambda, was solved by multiwavelength anomalous diffraction (MAD) for a selenomethionine (SeMet) derivative of the protein at 1.8 Angstrom resolution, using crystals in space group P2(1) [Yang et al. (2000), Nature Struct. Biol. 7, 230-237]. Subsequent analysis showed that the crystals of both the original protein and the SeMet derivative were pseudomerohedrally twinned with a twinning fraction similar or equal to 0.36, owing to the near-identity of the a and c axes. An analysis of the crystal structure solution is presented and the utility of twinned crystals for solving the structure using MAD and of different phasing strategies is discussed; the results obtained with several software packages are compared. [References: 21]

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