Femtosecond X-ray diffraction from two-dimensional protein crystals.

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 8.5?Å 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.

SUBMITTER: Frank M 

PROVIDER: S-EPMC4062087 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature