Abstract
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 8.5Å resolution for two different 2-D protein crystal samples each less than 10nm 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.
Original language | English (US) |
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Pages (from-to) | 95-100 |
Number of pages | 6 |
Journal | IUCrJ |
Volume | 1 |
DOIs | |
State | Published - Feb 28 2014 |
Keywords
- femtosecond crystallography
- membrane protein
- single layer X-ray diffraction
- two-dimensional protein crystal
ASJC Scopus subject areas
- General Chemistry
- Biochemistry
- General Materials Science
- Condensed Matter Physics