4.8 Article

X-ray Free Electron Lasers Motivate Bioanalytical Characterization of Protein Nanocrystals: Serial Femtosecond Crystallography

Journal

ANALYTICAL CHEMISTRY
Volume 85, Issue 7, Pages 3464-3471

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ac303716r

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Funding

  1. AMOS program, Office of Science, Office of Basic Energy Sciences (OBES), Division of Chemical Sciences, Geosciences, and Biosciences (CSGB) of the Department of Energy (DOE)
  2. SLAC Laboratory Directed Research and Development Program

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Atomic resolution structures of large biomacromolecular complexes can now be recorded at room temperature from crystals with submicrometer dimensions using intense femtosecond pulses delivered by the world's largest and most powerful X-ray machine, a laser called the Linac Coherent Light Source. Abundant opportunities exist for the bioanalytical sciences to help extend this revolutionary advance in structural biology to the ultimate goal of recording molecular-movies of noncrystalline biomacromolecules. This Feature will introduce the concept of serial femtosecond crystallography to the nonexpert, briefly review progress to date, and highlight some potential contributions from the analytical sciences.

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