Abstract
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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Acknowledgements
This work was supported by the European Union Integrated Project Biocrystallography (X) on a highly integrated technology platform for European Structural Genomics, the Spanish Ministry of Science and Innovation (grant BIO2006-06653), Fonds der Chemischen Industrie, Deutsche Forschungsgemeinschaft (DFG-IRTG1422) and the Max Planck Society. D.D.R. thanks Consejo Superior de Investigaciones Científicas for grant I3PMas_08_00057 for the Master in Crystallography and Crystallization, Universidad Internacional Menéndez Pelayo. We are also grateful to Institut d'Estadística de Catalunya for its contribution to grid computing.
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Rodríguez, D., Grosse, C., Himmel, S. et al. Crystallographic ab initio protein structure solution below atomic resolution. Nat Methods 6, 651–653 (2009). https://doi.org/10.1038/nmeth.1365
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DOI: https://doi.org/10.1038/nmeth.1365
