Abstract
Membrane proteins, including G protein-coupled receptors (GPCRs), constitute the most important drug targets. The increasing number of targets requires new structural information, which has proven tremendously challenging due to the difficulties in growing diffraction-quality crystals. Recent developments of serial femtosecond crystallography at X-ray free electron lasers combined with the use of membrane-mimetic gel-like matrix of lipidic cubic phase (LCP-SFX) for crystal growth and delivery hold significant promise to accelerate structural studies of membrane proteins. This chapter describes the development and current status of the LCP-SFX technology and elaborates its future role in structural biology of membrane proteins.
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Acknowledgments
This work was supported in parts by the NIH grants R01 GM108635 and U54 GM094618 (V.C.), NSF BioXFEL Science and Technology center grant 1231306 (U.W. and W.L.). Further supports were provided by the Arizona State University (ASU) Biodesign Seed Grant Program and ASU-Mayo Seed Grant Program (L.Z. and W.L.). Parts of this research were carried out at the LCLS, a National User Facility operated by Stanford University on behalf of the U.S. Department of Energy, Office of Basic Energy Sciences, and at the GM/CA CAT of the Argonne Photon Source, Argonne National Laboratory.
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Zhu, L., Weierstall, U., Cherezov, V., Liu, W. (2016). Serial Femtosecond Crystallography of Membrane Proteins. In: Moraes, I. (eds) The Next Generation in Membrane Protein Structure Determination. Advances in Experimental Medicine and Biology, vol 922. Springer, Cham. https://doi.org/10.1007/978-3-319-35072-1_11
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DOI: https://doi.org/10.1007/978-3-319-35072-1_11
Publisher Name: Springer, Cham
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