%0 Journal Article
%A Melnikov, Igor
%A Polovinkin, Vitaly
%A Kovalev, Kirill
%A Gushchin, Ivan
%A Shevtsov, Mikhail
%A Shevchenko, Vitaly
%A Mishin, Alexey
%A Alekseev, Alexey
%A Rodriguez-Valera, Francisco
%A Borshchevskiy, Valentin
%A Cherezov, Vadim
%A Leonard, Gordon A.
%A Gordeliy, Valentin
%A Popov, Alexander
%T Fast iodide-SAD phasing for high-throughput membrane protein structure determination
%J Science advances
%V 3
%N 5
%@ 2375-2548
%C Washington, DC [u.a.]
%I Assoc.
%M FZJ-2017-04109
%P e1602952
%D 2017
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:28508075
%U <Go to ISI:>//WOS:000401955300041
%R 10.1126/sciadv.1602952
%U https://juser.fz-juelich.de/record/834108