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Sci Adv. 2017 May 12;3(5):e1602952. doi: 10.1126/sciadv.1602952. eCollection 2017 May.

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

Author information

1
European Synchrotron Radiation Facility, 38043 Grenoble, France.
2
Institut de Biologie Structurale Jean-Pierre Ebel, Université Grenoble Alpes-Commissariat à l'Energie Atomique et aux Energies Alternatives-CNRS, F-38000 Grenoble, France.
3
Institute of Complex Systems (ICS), ICS-6, Structural Biochemistry, Research Centre Jülich, 52425 Jülich, Germany.
4
Moscow Institute of Physics and Technology, 141700 Dolgoprudny, Moscow Region, Russia.
5
Institute of Crystallography, University of Aachen (RWTH), Aachen, Germany.
6
Department of Vegetal Production and Microbiology, Universidad Miguel Hernández de Elche, San Juan de Alicante, Valencia, Spain.
7
Departments of Chemistry, Biological Sciences, and Physics & Astronomy, Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA.

Abstract

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.

KEYWORDS:

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

PMID:
28508075
PMCID:
PMC5429034
DOI:
10.1126/sciadv.1602952
[Indexed for MEDLINE]
Free PMC Article

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