Structure Gallery
High resolution membrane protein structures using Salipro® and CryoEM
Salipro® and CryoEM
Cryo-electron microscopy (cryoEM) is a cutting-edge technique used in drug discovery and structure-based drug design, as it can deliver key information on drug targets.
The Salipro® technology has been used to solve numerous high resolution structures of membrane proteins with cryoEM.
The images below showcase several of these structures, consisting of the membrane protein (yellow) and Salipro® scaffold protein (blue). In some cases, the membrane protein is bound to ligands (other colors). Click on the images below to learn more.
See our full publication list here.
D. Aydin, C.-T.Chien, J. Kreiter, et al.,Molecular mechanism of exchange coupling in CLC chloride/proton antiporters. Nat. Commun. (2026).
M. Lazarova, T. Eicher, C. Börnsen, et al., Conforma-tional plasticity across phylogenetic clusters of RND multidrug efflux pumps and its impact on substrate specificity. Nat. Commun. (2025).
M. Matusevicius, R. A. Corey, M. Gragera, K. Yamashita, T. Sprenger, et al., Insights from aquaporin structures into drug-resistant sleeping sickness. eLife14:RP107460 (2025).
D. Zhou, et al., Mechanistic insights into the acetyl-CoA recognition by SLC33A1. Cell Discov.11, 36 (2025).
M. T. K. Hankins, et al., MprF from Pseudomonas aeruginosa is a promiscuous lipid scramblase with broad substrate specificity. Sci. Adv.11,eads9135(2025).
S. Basse Hansen, et al., Structure of the [Ca]E2P intermediate of Ca2+-ATPase 1 from Listeria monocytogenes. EMBO Rep(2025).
D. Kurre, et al.,Structural insights into binding-site access and ligand recognition by human ABCB1. EMBO J. (2025).
H. Zhang, et al., Structural basis of augmenting taurine uptake by the taurine transporter in alleviating cellular senescence. Cell Research (2025).
W. Chojnacka, et al., Structural insights into GABAA receptor potentiation by Quaalude. Nat. Commun. 15, 5244 (2024).
S.T. Larsen, J.K. Dannersø, C. Juul Fælled Nielsen, et al., Conserved N-terminal Regulation of the ACA8 Calcium Pump with Two Calmodulin Binding Sites. J. Mol. Biol.436, 168747 (2024).
C. Fan, J. Cowgill, et al.,Divergent mechanisms of steroid inhibition in the human ρ1 GABAA receptor. Nat. Commun.15, 7795 (2024).
H. Chen, et al., Structural and functional insights into Spns2-mediated transport of sphingosine-1-phosphate. Cell186, 2644–2655, (2023).
J. Zhang, et al., Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10. Nat. Commun. 14, 6284 (2023).
S. Zhu, et al., Structural and dynamic mechanisms of GABAAreceptor modulators with opposing activities. Nat. Commun. 13, 4582 (2022).
C. M. Noviello, et al., Structural mechanisms of GABAA receptor autoimmune encephalitis. Cell 185, 2469-2477 (2022).
M. M. Rahman, et al., Structural mechanism of muscle nicotinic receptor desensitization and block by curare. Nat. Struct. Mol. Biol. 29, 386–394 (2022).
B. Xu, et al., Embigin facilitates monocarboxylate transporter 1 localization to the plasma membrane and transition to a decoupling state. Cell Reports40, 111343 (2022).
C. Wang, M. M. Polovitskaya, B. D. Delgado, T. J. Jentsch, S. B. Long, Gating choreography and mechanism of the human proton-activated chloride channel ASOR.Sci. Adv.8, 1–13 (2022).
C. M. Noviello, et al., Structure and gating mechanism of the a7 nicotinic acetylcholine receptor. Cell 184, 1–14 (2021).
Y. Zhang, et al., Asymmetric opening of the homopentameric 5-HT3A serotonin receptor in lipid bilayers. Nat. Commun. 12, 1074 (2021).
A. Ornik-cha, et al., Structural and functional analysis of the promiscuous AcrB and AdeB efflux pumps suggests different drug binding mechanisms. Nat. Commun. 12, 6919 (2021).
D.-M. Kehlenbeck, et al., Cryo-EM structure of MsbA in saposin-lipid nanoparticles ( Salipro ) provides insights into nucleotide coordination.FEBS J., 1–12 (2021).
L. Xiao, et al., Structures of the β-barrel assembly machine recognizing outer membrane protein substrates. FASEB J. 35, 1–13 (2021).
D. Du, et al., Interactions of a bacterial RND transporter with a transmembrane small protein in a lipid environment. Struct. Des., 1–10 (2020).
M. M. Rahman, et al., Structure of the Native Muscle-type Nicotinic Receptor and Inhibition by Snake Venom Toxins. Neuron, 1–11 (2020).
A. Gharpure, et al., Agonist Selectivity and Ion Permeation in the α3β4 Ganglionic Nicotinic Receptor.Neuron104, 501-511.e6 (2019).
R. Nagamura, et al., Structural basis for oligomerization of the prokaryotic peptide transporter PepT So2. Acta Crystallogr. Sect. F Struct. Biol. Commun. 75, 348–358 (2019).
N. X. Nguyen, et al., Cryo-EM structure of a fungal mitochondrial calcium uniporter. Nature 559, 570–574 (2018).
A. F. Kintzer, et al., Structural basis for activation of voltage sensor domains in an ion channel TPC1. Proc. Natl. Acad. Sci. U. S. A. 115, E9095–E9104 (2018).