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

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.

SUBMITTER: Melnikov I

PROVIDER: S-EPMC5429034 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

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

Melnikov Igor I Polovinkin Vitaly V Kovalev Kirill K Kovalev Kirill K Gushchin Ivan I Shevtsov Mikhail M Shevchenko Vitaly V Mishin Alexey A Alekseev Alexey A Rodriguez-Valera Francisco F Borshchevskiy Valentin V Cherezov Vadim V Leonard Gordon A GA Gordeliy Valentin V Popov Alexander A

Science advances 20170512 5

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 ...[more]

PMID: 28508075

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