4.8 Article

High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

Journal

SCIENCE
Volume 337, Issue 6092, Pages 362-364

Publisher

AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1217737

Keywords

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Funding

  1. LCLS Ultrafast Science Instruments (LUSI) project
  2. DOE, OBES
  3. Max Planck Society
  4. Hamburg Ministry of Science and Research
  5. Joachim Herz Stiftung, as part of the Hamburg Initiative for Excellence in Research (LEXI)
  6. Hamburg School for Structure and Dynamics in Infection
  7. U.S. NSF [0417142, MCB-1021557]
  8. NIH [1R01GM095583]
  9. German Federal Ministry for Education and Research [01KX0806, 01KX0807]
  10. Deutsche Forschungsgemeinschaft Cluster of Excellence [EXC 306]
  11. AMOS program within the Chemical Sciences, Geosciences, and Biosciences Division of the OBES, Office of Science, U.S. DOE
  12. Swedish Research Council
  13. Swedish Foundation for International Cooperation in Research and Higher Education
  14. Div Of Molecular and Cellular Bioscience
  15. Direct For Biological Sciences [1021557, 1120997] Funding Source: National Science Foundation

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Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

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