High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

  title={High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography},
  author={S. Boutet and L. Lomb and G. Williams and T. Barends and A. Aquila and R. Doak and U. Weierstall and D. DePonte and J. Steinbrener and R. Shoeman and M. Messerschmidt and A. Barty and T. White and S. Kassemeyer and R. Kirian and M. Seibert and P. Montanez and C. Kenney and R. Herbst and P. Hart and J. Pines and G. Haller and S. Gruner and H. Philipp and M. Tate and M. Hromalik and L. Koerner and N. van Bakel and J. Morse and W. Ghonsalves and D. Arnlund and M. Bogan and C. Caleman and R. Fromme and C. Hampton and M. Hunter and L. Johansson and G. Katona and C. Kupitz and M. Liang and A. V. Martin and K. Nass and L. Redecke and F. Stellato and N. T{\^i}mneanu and D. Wang and N. Zatsepin and D. Schafer and J. Defever and R. Neutze and P. Fromme and J. Spence and H. Chapman and I. Schlichting},
  pages={362 - 364}
Size Matters Less X-ray crystallography is a central research tool for uncovering the structures of proteins and other macromolecules. However, its applicability typically requires growth of large crystals, in part because a sufficient number of molecules must be present in the lattice for the sample to withstand x-ray—induced damage. Boutet et al. (p. 362, published online 31 May) now demonstrate that the intense x-ray pulses emitted by a free-electron laser source can yield data in few enough… Expand
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  • S. Gruner
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences
  • 2014
The latest tool in the crystallographic arsenal, the X-ray free electron laser (XFEL) promises to help surmount challenges, provided efficient ways are found to handle crystals in the demanding XFEL environment, and Cohen et al. (3) show that crystal handling technology developed primarily for use at synchrotron storage ringX-ray sources can also be effectively adapted for use in the XFel environment. Expand
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Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements.
Measurements indicate that current X-ray free-electron laser technology should enable structural determination from submicrometre protein crystals with atomic resolution, and the shortest apparent pulse lengths occur at the highest resolution. Expand
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  • R. Kirian, T. White, +12 authors J. Spence
  • Materials Science, Medicine
  • Acta crystallographica. Section A, Foundations of crystallography
  • 2011
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Radiation damage in protein serial femtosecond crystallography using an x-ray free-electron laser.
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Observation of decreased radiation damage at higher dose rates in room temperature protein crystallography.
Results of intensity-loss analysis unexpectedly showed that the dose tolerated by a crystal is dependent on the dose rate according to a positive linear relationship (99% correlation coefficient); a 60% increase in dose rate gave a 4-fold increase in crystal lifetime over the range studied. Expand