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.
Original language | English (US) |
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Pages (from-to) | 362-364 |
Number of pages | 3 |
Journal | Science |
Volume | 337 |
Issue number | 6092 |
DOIs | |
State | Published - Jul 20 2012 |
ASJC Scopus subject areas
- General