Fast native-SAD phasing for routine macromolecular structure determination

Nat Methods. 2015 Feb;12(2):131-3. doi: 10.1038/nmeth.3211. Epub 2014 Dec 15.


We describe a data collection method that uses a single crystal to solve X-ray structures by native SAD (single-wavelength anomalous diffraction). We solved the structures of 11 real-life examples, including a human membrane protein, a protein-DNA complex and a 266-kDa multiprotein-ligand complex, using this method. The data collection strategy is suitable for routine structure determination and can be implemented at most macromolecular crystallography synchrotron beamlines.

MeSH terms

  • Animals
  • DNA-Binding Proteins / chemistry*
  • Humans
  • Membrane Proteins / chemistry*
  • Models, Molecular
  • Multiprotein Complexes / chemistry*
  • Protein Conformation
  • Software
  • Synchrotrons
  • X-Ray Diffraction / methods*


  • DNA-Binding Proteins
  • Membrane Proteins
  • Multiprotein Complexes

Associated data

  • PDB/1XE1
  • PDB/1XG7
  • PDB/1YD7
  • PDB/2CVK
  • PDB/2I0X