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Fixed target matrix for femtosecond time-resolved and in situ serial micro-crystallography

DOI: 10.1063/1.4928706 DOI Help
PMID: 26798825 PMID Help

Authors: C. Mueller (University of Toronto) , Alexander Marx (Max Planck Society) , S. W. Epp (Max Planck Society) , Y. Zhong (Max Planck Society) , A. Kuo (University of Toronto) , A. R. Balo (University of Toronto) , J. Soman (Rice University) , F. Schotte (National Institute of Diabetes and Digestive and Kidney Diseases, USA) , H. T. Lemke (SLAC National Accelerator Laboratory) , Robin Owen (Diamond Light Source) , E. F. Pai (University of Toronto) , A. R. Pearson (University of Hamburg) , J. S. Olson (Rice University) , P. A. Anfinrud (National Institute of Diabetes and Digestive and Kidney Diseases, USA) , O. P. Ernst (University of Toronto) , R. J. Dwayne Miller (University of Toronto)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structural Dynamics , VOL 2

State: Published (Approved)
Published: September 2015
Diamond Proposal Number(s): 8367

Open Access Open Access

Abstract: We present a crystallography chip enabling in situ room temperature crystallography at microfocus synchrotron beamlines and X-ray free-electron laser (X-FEL) sources. Compared to other in situ approaches, we observe extremely low background and high diffraction data quality. The chip design is robust and allows fast and efficient loading of thousands of small crystals. The ability to load a large number of protein crystals, at room temperature and with high efficiency, into prescribed positions enables high throughput automated serial crystallography with microfocus synchrotron beamlines. In addition, we demonstrate the application of this chip for femtosecond time-resolved serial crystallography at the Linac Coherent Light Source (LCLS, Menlo Park, California, USA). The chip concept enables multiple images to be acquired from each crystal, allowing differential detection of changes in diffraction intensities in order to obtain high signal-to-noise and fully exploit the time resolution capabilities of XFELs.

Journal Keywords: Bragg reflection; Protein crystals; Crystal orientation

Subject Areas: Technique Development, Biology and Bio-materials

Instruments: I24-Microfocus Macromolecular Crystallography

Added On: 24/08/2015 12:33


Discipline Tags:

Technique Development - Life Sciences & Biotech Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)