Tricks of the trade used to accelerate high-resolution structure determination of membrane proteins

Sonoda, Yo; Cameron, Alex; Newstead, Simon; Omote, Hiroshi; Moriyama, Yoshinori; Kasahara, Michihiro; Iwata, So; Drew, David

doi:10.1016/j.febslet.2010.04.015

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Volume 584, Issue 12 , Pages 2539-2547, 18 June 2010

Tricks of the trade used to accelerate high-resolution structure determination of membrane proteins

Edited by Jan Rydström

Yo Sonoda
- Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK
- Present address: Drug Discovery Research Department, Central Research Laboratories, Kaken Pharmaceutical Co. Ltd, 14 Shinomiya-minamigawara, Yamashina, Kyoto 607-8042, Japan.
Alex Cameron
- Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Chilton, Oxfordshire OX11 0QX, UK
Simon Newstead
- Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK
- Present address: Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Hiroshi Omote
- Laboratory of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama 700-8530, Japan
Yoshinori Moriyama
- Laboratory of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama 700-8530, Japan
Michihiro Kasahara
- Laboratory of Biophysics, School of Medicine, Teikyo University, Hachioji, Tokyo 192-0395, Japan
So Iwata
- Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK
- Japan Science and Technology Agency, ERATO, Human Crystallography Project, Yoshida Konoe, Sakyo-ku, Kyoto 606-851, Japan
- Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Chilton, Oxfordshire OX11 0QX, UK
- Corresponding author at: Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK.
David Drew
- Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK
- Corresponding author.

Received 7 March 2010; received in revised form 1 April 2010; accepted 8 April 2010. published online 13 April 2010.

Abstract

The rate at which X-ray structures of membrane proteins are solved is on a par with that of soluble proteins in the late 1970s. There are still many obstacles facing the membrane protein structural community. Recently, there have been several technical achievements in the field that have started to dramatically accelerate structural studies. Here, we summarize these so-called ‘tricks-of-the-trade’ and include case studies of several mammalian transporters.

Abbreviations: SEC, size-exclusion chromatography, DDM, n-dodecyl-β-d-maltopyranoside, GFP, Green Fluorescent Protein, FSEC, fluorescence-detection size-exclusion chromatography, OG, n-octyl-β-d-maltopyranoside, OTG, n-octyl-β-d-thiomaltopyranoside, NM, n-nonyl-β-d-maltopyranoside, CPM, N-[4-(7-diethylamino-4-methyl-3-coumarinyl)phenyl]maleimide, TM, transmembrane, DM, n-decyl-β-d-maltopyranoside, CHS, cholesteryl hemisuccinate, TEV, tobacco etch virus protease, IMAC, immobilized metal affinity chromatography, Ni-NTA, nickel-nitrilotriacetic acid, C₁₂E₈, dodecyl octaethylene glycol ether, C₁₂E₉, dodecyl nonaethylene glycol ether, LDAO, n-dodecyl-N,N-dimethylamine-n-oxide, NG, n-nonyl-β-d-glucoside