Journal
SCIENCE
Volume 342, Issue 6165, Pages 1521-1524Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1244142
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Funding
- National Institutes of Health Common Fund in Structural Biology [P50 GM073197, P50 GM073210, R01 GM095583]
- National Institute of General Medical Sciences PSI: Biology [U54 GM094618, U54 GM094599]
- NSF Science and Technology Center [1231306]
- Helmholz Association
- German Research Foundation
- German Federal Ministry of Education and Research
- Science Foundation Ireland [07/IN.1/B1836, 12/IA/1255]
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X-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment.
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