Journal
SCIENCE
Volume 337, Issue 6092, Pages 362-364Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1217737
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Funding
- LCLS Ultrafast Science Instruments (LUSI) project
- DOE, OBES
- Max Planck Society
- Hamburg Ministry of Science and Research
- Joachim Herz Stiftung, as part of the Hamburg Initiative for Excellence in Research (LEXI)
- Hamburg School for Structure and Dynamics in Infection
- U.S. NSF [0417142, MCB-1021557]
- NIH [1R01GM095583]
- German Federal Ministry for Education and Research [01KX0806, 01KX0807]
- Deutsche Forschungsgemeinschaft Cluster of Excellence [EXC 306]
- AMOS program within the Chemical Sciences, Geosciences, and Biosciences Division of the OBES, Office of Science, U.S. DOE
- Swedish Research Council
- Swedish Foundation for International Cooperation in Research and Higher Education
- Div Of Molecular and Cellular Bioscience
- 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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