Serial Millisecond Crystallography of Membrane Proteins

  • Kathrin Jaeger
  • Florian Dworkowski
  • Przemyslaw Nogly
  • Christopher Milne
  • Meitian Wang
  • Joerg StandfussEmail author
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 922)


Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) is a powerful method to determine high-resolution structures of pharmaceutically relevant membrane proteins. Recently, the technology has been adapted to carry out serial millisecond crystallography (SMX) at synchrotron sources, where beamtime is more abundant. In an injector-based approach, crystals grown in lipidic cubic phase (LCP) or embedded in viscous medium are delivered directly into the unattenuated beam of a microfocus beamline. Pilot experiments show the application of microjet-based SMX for solving the structure of a membrane protein and compatibility of the method with de novo phasing. Planned synchrotron upgrades, faster detectors and software developments will go hand-in-hand with developments at free-electron lasers to provide a powerful methodology for solving structures from microcrystals at room temperature, ligand screening or crystal optimization for time-resolved studies with minimal or no radiation damage.


Serial crystallography High viscosity injector LCP injector Synchrotron Membrane proteins 



The work was financially supported by A Co-fund PSI Fellowship (to P.N.) and the SNSF project grant 31003A_141235 and 31003A_159558 (toJ.S.).


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Copyright information

© Springer International Publishing Switzerland 2016

Authors and Affiliations

  • Kathrin Jaeger
    • 1
  • Florian Dworkowski
    • 2
  • Przemyslaw Nogly
    • 1
  • Christopher Milne
    • 2
  • Meitian Wang
    • 2
  • Joerg Standfuss
    • 1
    Email author
  1. 1.Laboratory of Biomolecular ResearchPaul Scherrer InstituteVilligen PSISwitzerland
  2. 2.Swiss Light SourcePaul Scherrer InstituteVilligen PSISwitzerland

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