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Fixed target combined with spectral mapping: approaching 100% hit rates for serial crystallography

DOI: 10.1107/S2059798316010834 DOI Help

Authors: Saeed Oghbaey (University of Toronto) , Antoine Sarracini (University of Toronto) , Helen M. Ginn (University of Oxford; Diamond Light Source) , Olivier Pare-Labrosse (University of Toronto) , Anling Kuo (University of Toronto) , Alexander Marx (Max-Planck-Institute for the Structure and Dynamics of Matter) , Sascha W. Epp (Max-Planck-Institute for the Structure and Dynamics of Matter) , Darren A. Sherrell (Diamond Light Source) , Bryan T. Eger (University of Toronto) , Yinpeng Zhong (Max-Planck-Institute for the Structure and Dynamics of Matter) , Rolf Loch (Max-Planck-Institute for the Structure and Dynamics of Matter) , Valerio Mariani (Center for Free-Electron Laser Science, DESY) , Roberto Alonso-Mori (SLAC National Accelerator Laboratory) , Silke Nelson (SLAC National Accelerator Laboratory) , Henrik T. Lemke (SLAC National Accelerator Laboratory) , Robin L. Owen (Diamond Light Source) , Arwen R. Pearson (University of Hamburg) , David I. Stuart (Diamond Light Source) , Oliver P. Ernst (University of Hamburg) , Henrike Mueller-Werkmeister (University of Toronto; Max-Planck-Institute for the Structure and Dynamics of Matter) , R. J. Dwayne Miller (University of Toronto; Max-Planck-Institute for the Structure and Dynamics of Matter; University of Hamburg)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Structural Biology , VOL 72 , PAGES 944 - 955

State: Published (Approved)
Published: August 2016

Abstract: The advent of ultrafast highly brilliant coherent X-ray free-electron laser sources has driven the development of novel structure-determination approaches for proteins, and promises visualization of protein dynamics on sub-picosecond timescales with full atomic resolution. Significant efforts are being applied to the development of sample-delivery systems that allow these unique sources to be most efficiently exploited for high-throughput serial femtosecond crystallography. Here, the next iteration of a fixed-target crystallography chip designed for rapid and reliable delivery of up to 11 259 protein crystals with high spatial precision is presented. An experimental scheme for predetermining the positions of crystals in the chip by means of in situ spectroscopy using a fiducial system for rapid, precise alignment and registration of the crystal positions is presented. This delivers unprecedented performance in serial crystallography experiments at room temperature under atmospheric pressure, giving a raw hit rate approaching 100% with an effective indexing rate of approximately 50%, increasing the efficiency of beam usage and allowing the method to be applied to systems where the number of crystals is limited.

Journal Keywords: femtosecond time-resolved crystallography; high-throughput serial crystallography; fixed-target sample delivery; room-temperature crystallography

Subject Areas: Technique Development, Biology and Bio-materials

Technical Areas: Detectors

Added On: 17/11/2016 10:48

Discipline Tags:

Technique Development - Life Sciences & Biotech Life Sciences & Biotech

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