期刊
NATURE METHODS
卷 13, 期 4, 页码 345-351出版社
NATURE PORTFOLIO
DOI: 10.1038/NMETH.3801
关键词
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资金
- European Molecular Biology Organization (EMBO)
- Swedish Research Council [2014-5583, 2013-3922, 2013-4621, 2010-4483]
- Knut and Alice Wallenberg Foundation [2014.0112]
- Swedish Cancer Society [13 0401, 14 0473]
- Swedish Childhood Cancer Foundation [PR2014-0156]
- Nanyang Technological University
- Marie Curie Actions Project FP7-People-ITN [235649]
- Stiftelsen Lakare mot AIDS Forskningsfond
- Howard Hughes Medical Institute
- US National Institutes of Health [R01GM098672, P50GM082250, 1S100D020054]
- Karolinska Institutet Center for Biosciences
- China Scholarship Council
- Molecular Medicine Partnership Unit (MMPU) of the University Clinic Heidelberg
- European Molecular Biology Laboratory
A limiting factor in membrane protein research is the ability to solubilize and stabilize such proteins. Detergents are used most often for solubilizing membrane proteins, but they are associated with protein instability and poor compatibility with structural and biophysical studies. Here we present a saposin-lipoprotein nanoparticle system, Salipro, which allows for the reconstitution of membrane proteins in a lipid environment that is stabilized by a scaffold of saposin proteins. We demonstrate the applicability of the method on two purified membrane protein complexes as well as by the direct solubilization and nanoparticle incorporation of a viral membrane protein complex from the virus membrane. Our approach facilitated high-resolution structural studies of the bacterial peptide transporter PeptT(S02) by single-particle cryo-electron microscopy (cryo-EM) and allowed us to stabilize the HIV envelope glycoprotein in a functional state.
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