June 1, 2009 - Volume 87, Number 22
- p. 27
Science & Technology
Paul Kenis
Mini Mixer Bacteriorhodopsin crystals (right) are grown by this device, which injects a total of 20 nanoliters of aqueous protein solution (brown droplets injected from right and left) into a lipid reservoir. This video shows the device in action.
More Science & Technology Concentrates
- Finding Crystallization Sweet Spots
- Automated device mixes nanoliter quantities of membrane-protein components.
- Probing More Of That Vast Chemical Space
- Including chemical scaffolds in libraries aids screening.
- Magnetic Nanopropellers On The Move
- Microscopic swimmers can be propelled wirelessly.
- Oak Barrel Provenance Alters Wine Chemistry
- Geographic traits in barrel woods shape wine's complexity.
- Directing Fluorination Differently
- After fluorination, directing group can be transformed to make a range of F-containing molecules.
- An Easier Way To Model Hydrate Lattices
- New method streamlines computations by focusing on likely structures.
- Antifouling Agent Linked To Endangered Fish Deformities
- Study implicates triphenyltin in Chinese sturgeon abnormalities.
- A Simpler Route To Multifunctional Nanocomposites
- Viruses serve as biological templates for nanoscale heterostructures.
Topics Covered
Membrane proteins play critical roles in cell signaling and energy transduction, so knowing their crystal structures could help scientists better understand how cells work while also pointing toward new treatments for diseases that involve these proteins. Relatively few membrane-protein structures have been determined, however, because they are notoriously difficult to crystallize and the pure proteins tend to be available only in minute quantities. What's more, today's crystallization methods do not allow experimental conditions to be easily varied, a feature that would hasten the identification of practical crystallization conditions for a particular protein. Now, Sarah L. Perry, Paul J. A. Kenis, and coworkers at the University of Illinois, Urbana-Champaign, have developed a device that enables them to screen crystallization conditions by mixing various compositions and concentrations of aqueous protein solutions and viscous lipids in 20-nanoliter batches (Cryst. Growth Des., DOI: 10.1021/cg900289d). The pneumatically actuated mixer uses just one-thousandth of the material consumed by today's microscale screening tools. In a proof-of-concept experiment, the team used the device to grow crystals of bacteriorhodopsin, a membrane protein commonly used for benchmarking.
- Chemical & Engineering News
- ISSN 0009-2347
- Copyright © 2009 American Chemical Society
Mini Mixer
Bacteriorhodopsin crystals (right) are grown by this device, which injects a total of 20 nanoliters of aqueous protein solution (brown droplets injected from right and left) into a lipid reservoir.
Paul Kenis- Chemical & Engineering News
- ISSN 0009-2347
- Copyright © 2009 American Chemical Society
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