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  Serial Synchrotron Cryallography with a Fixed Target

Müller-Werkmeister, H., Schulz, E.-C., Sherrell, D., Axford, D., Tellkamp, F., Owen, R. L., et al. (2017). Serial Synchrotron Cryallography with a Fixed Target. Biophysical Journal, 112, 579A-579A. doi:10.1016/j.bpj.2016.11.3117.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-9E5F-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-9E60-1
Genre: Conference Paper

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1-s2.0-S0006349516341479-main.pdf (Publisher version), 42KB
 
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https://doi.org/10.1016/j.bpj.2016.11.3117 (Publisher version)
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 Creators:
Müller-Werkmeister, H.1, Author              
Schulz, E.-C.1, Author              
Sherrell, D.2, Author
Axford, D.2, Author
Tellkamp, F.3, Author              
Owen, R. L.2, Author
Miller, R. J. D.1, Author              
Affiliations:
1Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
2Diamond Light Source, Didcot, ou_persistent22              
3Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_2074322              

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 Abstract: Serial crystallography has been driven mainly from sample requirements imposed by X-ray free electron lasers, however there is huge potential for new applications and experiments as well at regular (microfocus) synchrotron beamlines normally used for rotation based structure determination from single protein crystals. Our approach uses a combination of fixed target arrays for sample delivery of micron sized protein crystals and a fast, accurate translation system and thus allows high throughput serial data collection at high hit-rates and with low sample consumption. Data obtained in this approach yield high resolution structures and are collected at at room temperature with a low radiation dose per individual crystal, highly desirable for many proteins, where structures can normally suffer from radiation damage. Further the possibility to extend the approach to time-resolved crystallography for the study of protein dynamics on the millisecond timescale is shown.

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Language(s): eng - English
 Dates: 2017-02-032017-02-03
 Publication Status: Published in print
 Pages: 1
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 Table of Contents: -
 Rev. Method: Internal
 Identifiers: DOI: 10.1016/j.bpj.2016.11.3117
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Title: 58th Annual Meeting of the Biophysical-Society
Place of Event: San Francisco, CA
Start-/End Date: 2014-02-15 - 2014-02-19

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Title: Biophysical Journal
  Other : Biophys. J.
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press, 3
Pages: - Volume / Issue: 112 Sequence Number: - Start / End Page: 579A - 579A Identifier: Other: 0006-3495
CoNE: /journals/resource/954925385117