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

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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.

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  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: uson@ibmb.csic.es



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