Popular Articles
- Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature
- NSF awards $22.5 million to capture biology at the atomic level using X-ray lasers
- BioXFEL Research Support Call for Proposals
- Frankuchen Award : ACA 2019
- UWM researchers create first 3D movie of virus in action
Archived Articles
- Details
- Thursday, 02 July 2015
Serial methods for crystallography have the potential to enable dynamic structural studies of protein targets that have been resistant to single-crystal strategies. The use of serial data-collection strategies can circumvent challenges associated with radiation damage and repeated reaction initiation. This work utilizes a microfluidic crystallization platform for the serial time-resolved Laue diffraction analysis of macroscopic crystals of photoactive yellow protein (PYP).
Towards time-resolved serial crystallography in a microfluidic device.
Ashtamurthy S. Pawate, Vukica Srajer, Jeremy Schieferstein, Sudipto Guha, Robert Henning, Irina Kosheleva, Marius Schmidt, Zhong Ren, Paul J. A. Kenisa and Sarah L. Perrya
See full publication here.
Serial methods for crystallography have the potential to enable dynamic structural studies of protein targets that have been resistant to single-crystal strategies. The use of serial data-collection strategies can circumvent challenges associated with radiation damage and repeated reaction initiation. This work utilizes a microfluidic crystallization platform for the serial time-resolved Laue diffraction analysis of macroscopic crystals of photoactive yellow protein (PYP). Reaction initiation was achieved via pulsed laser illumination, and the resultant electron-density difference maps clearly depict the expected pR1/pRE46Q and pR2/pRCW states at 10 ms and the pB1 intermediate at 1 ms. The strategies presented here have tremendous potential for extension to chemical triggering methods for reaction initiation and for extension to dynamic, multivariable analyses.
