Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.8
Classification:SIGNALING PROTEIN, ELECTRON TRANSPORT
Release Date:2013-12-18
Deposition Date:2013-10-23
Revision Date:2014-01-22#2017-06-07#2018-02-14
Molecular Weight:53259.86
Macromolecule Type:Protein
Residue Count:430
Atom Site Count:3116
DOI:10.2210/pdb4nc3/pdb
Abstract:
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.
Resolution:2.8
Classification:SIGNALING PROTEIN, ELECTRON TRANSPORT
Release Date:2013-12-18
Deposition Date:2013-10-23
Revision Date:2014-01-22#2017-06-07#2018-02-14
Molecular Weight:53259.86
Macromolecule Type:Protein
Residue Count:430
Atom Site Count:3116
DOI:10.2210/pdb4nc3/pdb
Abstract:
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.
| Date made available | 2013 |
|---|---|
| Publisher | RCSB-PDB |