High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography
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 (XF...
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Veröffentlicht in: | Science (American Association for the Advancement of Science) 2012-07, Vol.337 (6092), p.362-364 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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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ISSN: | 0036-8075 1095-9203 1095-9203 |
DOI: | 10.1126/science.1217737 |