| Home > Publications database > High-resolution protein structure determination by serial femtosecond crystallography |
| Journal Article/Journal Article | PHPPUBDB-22476 |
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2012
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Please use a persistent id in citations: doi:10.1126/science.1217737
Abstract: 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.
Keyword(s): Animals (MeSH) ; Crystallography, X-Ray: methods (MeSH) ; Lasers (MeSH) ; Muramidase: chemistry (MeSH) ; Muramidase: radiation effects (MeSH) ; Protein Conformation (MeSH) ; hen egg lysozyme ; Muramidase
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