Abstract Details 144

Fixed Target 2D and 3D Protein Crystallography at XFELs
Abstract ID 144
Presenter Matthias Frank
Presentation Type Poster
Full Author List

Henry Benner, Matt Coleman, Stefan Hau-Riege, Mark Hunter, Tom Pardini, Brent Segelke (Lawrence Livermore National Laboratory)

James Evans (Pacific Northwest National Laboratory)

John Spence, Nadia Zatsepin, Yun Zhao, Petra Fromme, Jay-How Yang (Arizona State University)

Xioadan Li, Ching-Ju Tsai, Bill Pedrini, Celestinio Padeste, Gebhard Schertler (Paul Scherrer Institut)

Anton Barty, Rick Kirian, Henry Chapman (Centre for Free-electron Laser Science, DESY)

Sebastien Boutet, Garth Williams, Marc Messerschmitt, Marvin Seibert (LCLS/SLAC)


Lawrence Livermore National Laboratory


Serial femtosecond nanocrystallography (SFX) has been demonstrated successfully in a number of experiments at LCLS and SACLA over the last years. Most SFX applications to date have used 3-dimensional nano- or microcrystals and utilize a liquid-jet based sample introduction approach that requires large amounts of sample and/or are not conducive to measuring 2-dimensional (2D) protein crystals. 2D crystallography of membrane proteins has been developed originally in cryoelectron microscopy and is an avenue for obtaining structural information on membrane proteins that do not easily form 3D crystals. Here we describe a fixed target approach for 2D and 3D crystallography at XFELs that allows diffraction measurements on samples supported by thin substrates at room temperature. We present first promising results from experiments at LCLS that included 2D crystal samples of the membrane protein bacteriorhodopsin and 3D microcrystal samples of REP24, a soluble protein. We discuss strategies for reducing amounts of required sample and increasing speed of data acquisition further to render this approach a viable alternative to the liquid-jet based sample introduction approaches. The fixed-target approach is expected to open up new opportunities for time-resolved SFX on samples that are not abundant and/or require the sample to be flat.



Funding Acknowledgement