| Structural highlights
Publication Abstract from PubMed
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.
Fast iodide-SAD phasing for high-throughput membrane protein structure determination.,Melnikov I, Polovinkin V, Kovalev K, Gushchin I, Shevtsov M, Shevchenko V, Mishin A, Alekseev A, Rodriguez-Valera F, Borshchevskiy V, Cherezov V, Leonard GA, Gordeliy V, Popov A Sci Adv. 2017 May 12;3(5):e1602952. doi: 10.1126/sciadv.1602952. eCollection 2017, May. PMID:28508075[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Melnikov I, Polovinkin V, Kovalev K, Gushchin I, Shevtsov M, Shevchenko V, Mishin A, Alekseev A, Rodriguez-Valera F, Borshchevskiy V, Cherezov V, Leonard GA, Gordeliy V, Popov A. Fast iodide-SAD phasing for high-throughput membrane protein structure determination. Sci Adv. 2017 May 12;3(5):e1602952. doi: 10.1126/sciadv.1602952. eCollection 2017, May. PMID:28508075 doi:http://dx.doi.org/10.1126/sciadv.1602952
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