Brief Communication abstract

Nature Methods 6, 651 - 653 (2009)
Published online: 16 August 2009 | doi:10.1038/nmeth.1365

Crystallographic ab initio protein structure solution below atomic resolution

Dayté D Rodríguez1,5, Christian Grosse2,5, Sebastian Himmel3, César González1, Iñaki M de Ilarduya1, Stefan Becker3, George M Sheldrick2 & Isabel Usón1,4


Ab initio macromolecular phasing has been so far limited to small proteins diffracting at atomic resolution (beyond 1.2 Å) unless heavy atoms are present. We describe a general ab initio phasing method for 2 Å data, based on combination of localizing model fragments such as small á-helices with Phaser and density modification with SHELXE. We implemented this approach in the program Arcimboldo to solve a 222-amino-acid structure at 1.95 Å.

  1. Instituto de Biología Molecular de Barcelona, Barcelona Science Park, Barcelona, Spain.
  2. Lehrstuhl für Strukturchemie, Universität Göttingen, Göttingen, Germany.
  3. Max Planck Institute for Biophysical Chemistry, Department of NMR-based Structural Biology, Göttingen, Germany.
  4. Institució Catalana de Recerca i Estudis Avançats, Barcelona, Spain.
  5. These authors contributed equally to this work.

Correspondence to: Isabel Usón1,4 e-mail:


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