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Nat Methods ; 11(7): 734-6, 2014 Jul.
Article in English | MEDLINE | ID: mdl-24813624

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.


Subject(s)
Crystallography/methods , Electron Transport Complex IV/chemistry , Lasers , Animals , Cattle , Electron Transport Complex IV/radiation effects
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