Research ArticleBIOCHEMISTRY

Fast iodide-SAD phasing for high-throughput membrane protein structure determination

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Science Advances  12 May 2017:
Vol. 3, no. 5, e1602952
DOI: 10.1126/sciadv.1602952

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We describe a fast, easy, and potentially universal method for the de novo solution of the crystal structures of membrane proteins via iodide–single-wavelength anomalous diffraction (I-SAD). The potential universality of the method is based on a common feature of membrane proteins—the availability at the hydrophobic-hydrophilic interface of positively charged amino acid residues with which iodide strongly interacts. We demonstrate the solution using I-SAD of four crystal structures representing different classes of membrane proteins, including a human G protein–coupled receptor (GPCR), and we show that I-SAD can be applied using data collection strategies based on either standard or serial x-ray crystallography techniques.

  • Membrane protein
  • x-ray crystallography
  • experimental phasing
  • serial crystallography
  • SAD
  • iodide

This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license, which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.

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