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Title: Femtosecond X-ray Diffraction From Two-Dimensional Protein Crystals

Here we present femtosecond x-ray diffraction patterns from two-dimensional (2-D) protein crystals using an x-ray free electron laser (XFEL). To date it has not been possible to acquire x-ray diffraction from individual 2-D protein crystals due to radiation damage. However, the intense and ultrafast pulses generated by an XFEL permits a new method of collecting diffraction data before the sample is destroyed. Utilizing a diffract-before-destroy methodology at the Linac Coherent Light Source, we observed Bragg diffraction to better than 8.5 Å resolution for two different 2-D protein crystal samples that were maintained at room temperature. These proof-of-principle results show promise for structural analysis of both soluble and membrane proteins arranged as 2-D crystals without requiring cryogenic conditions or the formation of three-dimensional crystals.
 [1] ;  [2] ;  [1] ;  [3] ;  [2] ;  [4] ;  [5] ;  [1] ;  [6] ;  [1] ;  [1] ;  [5] ;  [7] ;  [1] ;  [7] ;  [1] ;  [2] ;  [4] ;  [7] ;  [6] more »;  [7] ;  [7] ;  [2] ;  [1] ;  [8] « less
  1. Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
  2. Univ. of California, Davis, CA (United States)
  3. SLAC National Accelerator Lab., Menlo Park, CA (United States). Linac Coherent Light Source (LCLS)
  4. Arizona State Univ., Tempe, AZ (United States)
  5. Univ. of Hamburg (Germany)
  6. Center for Biophotonics, Sacramento, CA (United States)
  7. Paul Scherrer Inst., Villigen (Switzerland)
  8. Pacific Northwest National Lab. (PNNL), Richland, WA (United States); Univ. of California, Davis, CA (United States)
Publication Date:
OSTI Identifier:
Report Number(s):
Journal ID: ISSN 2052-2525; KP1704020
DOE Contract Number:
Resource Type:
Journal Article
Resource Relation:
Journal Name: IUCrJ; Journal Volume: 1
International Union of Crystallography
Research Org:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Org:
Country of Publication:
United States