Journal Article

FZJ-2017-04109

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Fast iodide-SAD phasing for high-throughput membrane protein structure determination

Melnikov, I. ; Polovinkin, V. ; Kovalev, K.FZJ* ; Gushchin, I. ; Shevtsov, M. ; Shevchenko, V.FZJ* ; Mishin, A. ; Alekseev, A. ; Rodriguez-Valera, F. ; Borshchevskiy, V. ; Cherezov, V. ; Leonard, G. A. ; Gordeliy, V. (Corresponding author)FZJ* ; Popov, A.

2017
Assoc. Washington, DC [u.a.]

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Please use a persistent id in citations: http://hdl.handle.net/2128/15139  doi:10.1126/sciadv.1602952

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.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)

Appears in the scientific report 2017

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Database coverage:
; ; ; ; DOAJ Seal ; Emerging Sources Citation Index ; NCBI Molecular Biology Database ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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