Abstract
We report a method of femtosecond crystallography for solving radiation damage-free crystal structures of large proteins at sub-angstrom spatial resolution, using a large single crystal and the femtosecond pulses of an X-ray free-electron laser (XFEL). We demonstrated the performance of the method by determining a 1.9-Å radiation damage-free structure of bovine cytochrome c oxidase, a large (420-kDa), highly radiation-sensitive membrane protein.
Original language | English |
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Pages (from-to) | 734-736 |
Number of pages | 3 |
Journal | Nature Methods |
Volume | 11 |
Issue number | 7 |
DOIs | |
Publication status | Published - Jul 2014 |
ASJC Scopus subject areas
- Biotechnology
- Biochemistry
- Molecular Biology
- Cell Biology