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Sökning: WFRF:(Kupitz Christopher) > (2013)

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1.
  • Johansson, Linda C, 1983, et al. (författare)
  • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography.
  • 2013
  • Ingår i: Nature communications. - : Springer Science and Business Media LLC. - 2041-1723. ; 4
  • Tidskriftsartikel (refereegranskat)abstract
    • Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8Å resolution and determine its serial femtosecond crystallography structure to 3.5Å resolution. Although every microcrystal is exposed to a dose of 33MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.
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2.
  • Liu, Wei, et al. (författare)
  • Serial Femtosecond Crystallography of G Protein-Coupled Receptors
  • 2013
  • Ingår i: Science. - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 342:6165, s. 1521-1524
  • Tidskriftsartikel (refereegranskat)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.
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