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

Science Advances
Igor MelnikovAlexander Popov

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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Citations

May 20, 2017·Science·Ivan GushchinValentin Gordeliy
Jan 10, 2018·Frontiers in Pharmacology·Byron Carpenter, Guillaume Lebon
Sep 30, 2017·Chembiochem : a European Journal of Chemical Biology·Tianyuan PengNicola L B Pohl
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Dec 9, 2017·Journal of Applied Crystallography·Gianluca SantoniAlexander Popov
Oct 17, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Ruyin CaoPaolo Carloni
Oct 3, 2018·Communications Biology·Chia-Ying HuangMeitian Wang
Apr 16, 2019·F1000Research·Igor E EliseevOleg B Chakchir
Dec 20, 2020·The FEBS Journal·Ali A Kermani
Dec 17, 2020·MSystems·Mario López-PérezFrancisco Rodriguez-Valera
Mar 23, 2021·Critical Reviews in Microbiology·Lucindo Cardoso de PinaL Caetano M Antunes
May 15, 2021·Frontiers in Molecular Biosciences·Hung N DoYinglong Miao
May 26, 2021·Scientific Reports·Yury L RyzhykauValentin I Gordeliy

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Methods Mentioned

BETA
x-ray crystallography
size-exclusion chromatography

Software Mentioned

Coot
SigAno
DANO
AIMLESS
SHELXE
XSCALE
autobuild
CCP4
BEST
FFT

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