Journal
IUCRJ
Volume 1, Issue -, Pages 95-100Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2052252514001444
Keywords
two-dimensional protein crystal; femtosecond crystallography; single layer X-ray diffraction; membrane protein
Funding
- US Department of Energy by Lawrence Livermore National Laboratory [DE-AC52-07NA27344]
- Pacific Northwest National Laboratory [DE-AC05-76RL01830]
- UCOP Lab Fee Program [118036]
- NIH [5RC1GM091755]
- NSF award [MCB-1021557]
- NSF STC award [1231306]
- LLNL Lab-Directed Research and Development Project [012-ERD-031]
- PNNL Chemical Imaging Initiative
- Center for Biophotonics Science and Technology, NSF Science and Technology Center [PHY0120999]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1021557] Funding Source: National Science Foundation
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X-ray diffraction patterns from two-dimensional (2-D) protein crystals obtained using femtosecond X-ray pulses from an X-ray free-electron laser (XFEL) are presented. To date, it has not been possible to acquire transmission X-ray diffraction patterns from individual 2-D protein crystals due to radiation damage. However, the intense and ultrafast pulses generated by an XFEL permit a new method of collecting diffraction data before the sample is destroyed. Utilizing a diffract-before-destroy approach at the Linac Coherent Light Source, Bragg diffraction was acquired to better than 8.5 angstrom resolution for two different 2-D protein crystal samples each less than 10 nm thick and 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.
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