4.8 Article

Determination of damage-free crystal structure of an X-ray-sensitive protein using an XFEL

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NATURE METHODS
卷 11, 期 7, 页码 734-U174

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NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.2962

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资金

  1. X-ray Free Electron Laser Priority Strategy Program (The Ministry of Education, Culture, Sports, Science and Technology in Japan (MEXT))
  2. JST/CREST
  3. MEXT/Japan Society for the Promotion of Science (JSPS) [24000018]
  4. Japan Synchrotron Radiation Research Institute (JASRI) [2012A8011, 2012B8040, 2013A8047, 2013B8052]
  5. Grants-in-Aid for Scientific Research [22370060, 26291033, 25109540, 24000018, 26104532] Funding Source: KAKEN

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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-angstrom radiation damage-free structure of bovine cytochrome c oxidase, a large (420-kDa), highly radiation-sensitive membrane protein.

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