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  Protein crystals IR laser ablated from aqueous solution at high speed retain their diffractive properties: applications in high-speed serial crystallography

Schulz, E.-C., Kaub, J., Busse, F., Mehrabi, P., Müller-Werkmeister, H., Pai, E. F., et al. (2017). Protein crystals IR laser ablated from aqueous solution at high speed retain their diffractive properties: applications in high-speed serial crystallography. Journal of Applied Crystallography, 50, 1773-1781. doi:10.1107/S1600576717014479.

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 Creators:
Schulz, Eike-Christian1, Author           
Kaub, Johannes1, Author           
Busse, Frederik1, Author           
Mehrabi, Pedram2, 3, Author
Müller-Werkmeister, Henrike1, Author           
Pai, Emil F.2, 3, 4, 5, Author
Robertson, Wesley1, Author           
Miller, R. J. Dwayne1, 6, 7, Author           
Affiliations:
1Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
2Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada, ou_persistent22              
3The Campbell Family Cancer Research Institute, Ontario Cancer Institute, Toronto, Ontario, Canada, ou_persistent22              
4Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada, ou_persistent22              
5eDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada, ou_persistent22              
6Department of Physics, Centre for Ultrafast Imaging – University of Hamburg, Luruper Chaussee 149, Hamburg, 22761, Germany, ou_persistent22              
7Departments of Chemistry and Physics, University of Toronto, 80 St George Street, Toronto M5S 1H6, Ontario, Canada, ou_persistent22              

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Free keywords: serial synchrotron crystallography; SSX; picosecond infrared lasers; PIRL; fixed targets; sample delivery
 Abstract: In order to utilize the high repetition rates now available at X-ray free-electron laser sources for serial crystallography, methods must be developed to softly deliver large numbers of individual microcrystals at high repetition rates and high speeds. Picosecond infrared laser (PIRL) pulses, operating under desorption by impulsive vibrational excitation (DIVE) conditions, selectively excite the OH vibrational stretch of water to directly propel the excited volume at high speed with minimized heating effects, nucleation formation or cavitationinduced shock waves, leaving the analytes intact and undamaged. The soft nature and laser-based sampling flexibility provided by the technique make the PIRL system an interesting crystal delivery approach for serial crystallography. This paper demonstrates that protein crystals extracted directly from aqueous buffer solution via PIRL-DIVE ablation retain their diffractive properties and can be usefully exploited for structure determination at synchrotron sources. The remaining steps to implement the technology for high-speed serial femtosecond crystallography, such as single-crystal localization, high-speed sampling and synchronization, are described. This proof-of-principle experiment demonstrates the viability of a new laser-based high-speed crystal delivery system without the need for liquid-jet injectors or fixed-target mounting solutions.

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Language(s): eng - English
 Dates: 2017-05-242017-10-062017-11-202017-12
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S1600576717014479
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Title: Journal of Applied Crystallography
  Abbreviation : J. Appl. Cryst.
Source Genre: Journal
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Publ. Info: Oxford, England : Blackwell Publishing on behalf of the International Union of Crystallography
Pages: - Volume / Issue: 50 Sequence Number: - Start / End Page: 1773 - 1781 Identifier: ISSN: 0021-8898
CoNE: https://pure.mpg.de/cone/journals/resource/954925410812