Wayne Hendrickson discusses the consortium efforts and developments in methodology that in recent years have allowed unprecedented advances in atomic-structure determination of membrane proteins.
Abstract
Membrane proteins are substantially more challenging than natively soluble proteins as subjects for structural analysis. Thus, membrane proteins are greatly underrepresented in structural databases. Recently, focused consortium efforts and advances in methodology for protein production, crystallographic analysis and cryo-EM analysis have accelerated the pace of atomic-level structure determination of membrane proteins.
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Acknowledgements
I thank Y. Guo for producing Figure 2 and Y. Shi for providing a high-resolution image for Figure 3b. I thank F. Mancia, Q. Liu, L. Shapiro, B. Kloss, R. Bruni, R. Kalathur and others from the NYCOMPS team for numerous contributions to the experience reported here. This work was supported in part by NIH grants GM095315 and GM107462.
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Hendrickson, W. Atomic-level analysis of membrane-protein structure. Nat Struct Mol Biol 23, 464–467 (2016). https://doi.org/10.1038/nsmb.3215
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DOI: https://doi.org/10.1038/nsmb.3215
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