In Situ Serial Laue Diffraction on a Microfluidic Crystallization Device

Journal of Applied Crystallography 47
November 18, 2014

Renewed interest in room-temperature diffraction has been prompted by the desire to observe structural dynamics of proteins as they function. Serial crystallography, an experimental strategy that aggregates small pieces of data from a large uniform pool of crystals, has been demonstrated at synchrotrons and X-ray free-electron lasers. This work utilizes a microfluidic crystallization platform for serial Laue diffraction from macroscopic crystals and proposes that a collection of small slices of Laue data from many individual crystals is a realistic solution to the difficulties in dynamic studies of irreversible biochemical reactions.

Perry, S. L., Guha, S., Pawate, A. S., Henning, R., Kosheleva, I., Srajer, V., Kenis, P. J. A., and Ren, Z.
In Situ Serial Laue Diffraction on a Microfluidic Crystallization Device
Journal of Applied Crystallography 47, 1975-1982 (2014)
abstract