Journal article
Automated microfluidic sample-preparation platform for high-throughput structural investigation of proteins by small-angle X-ray scattering
A new microfluidic sample-preparation system is presented for the structural investigation of proteins using small-angle X-ray scattering (SAXS) at synchrotrons. The system includes hardware and software features for precise fluidic control, sample mixing by diffusion, automated X-ray exposure control, UV absorbance measurements and automated data analysis.
As little as 15 l of sample is required to perform a complete analysis cycle, including sample mixing, SAXS measurement, continuous UV absorbance measurements, and cleaning of the channels and X-ray cell with buffer. The complete analysis cycle can be performed in less than 3 min. Bovine serum albumin was used as a model protein to characterize the mixing efficiency and sample consumption of the system.
The N2 fragment of an adaptor protein (p120-RasGAP) was used to demonstrate how the device can be used to survey the structural space of a protein by screening a wide set of conditions using high-throughput techniques. © 2011 International Union of Crystallography.
Language: | English |
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Year: | 2011 |
Pages: | 1090-1099 |
ISSN: | 16005767 and 00218898 |
Types: | Journal article |
DOI: | 10.1107/S0021889811030068 |
ORCIDs: | 0000-0001-8011-6414 and 0000-0002-4694-4299 |
Automated data analysis Automation Body fluids Bovine serum albumins Data reduction Fluidic control Hardware and software High-throughput High-throughput technique Microfluidics Mixing by diffusion Mixing efficiency Model proteins Protein structure Proteins Sample consumption Scattering Small-angle X-ray scattering Structural analysis Structural investigation UV absorbance X ray scattering