A modified method for determining the three-dimensional structure of large proteins seems to show them in a more natural pose than conventional techniques do.
Proteins called G protein-coupled receptors (GPCRs) are important drug targets, but researchers struggle to figure out their structures. Vadim Cherezov of the Scripps Research Institute in La Jolla, California, and his colleagues modified the standard X-ray crystallography technique by using an X-ray free-electron laser to capture serial images of the structure of a GPCR for the neurotransmitter serotonin.
The team used the technique on tiny serotonin-receptor crystals kept at room temperature, and obtained structures that differed from those determined using conventional approaches with larger crystals kept at cool temperatures. The results suggest that the room-temperature free-electron-laser approach may better capture the protein's conformation in its native environment.
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Better pictures of protein structures. Nature 505, 135 (2014). https://doi.org/10.1038/505135c
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DOI: https://doi.org/10.1038/505135c
