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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.
Original languageEnglish
JournalJournal of Applied Crystallography
Issue number5
Pages (from-to)1090-1099
StatePublished - 2011
CitationsWeb of Science® Times Cited: 20


  • High-throughput, UV absorbance, Mixing efficiency, Automated data analysis, Structural analysis, Automation, Model proteins, Hardware and software, Data reduction, Structural investigation, Fluidic control, Protein structure, Microfluidics, Scattering, X ray scattering, Bovine serum albumins, Sample consumption, Proteins, High-throughput technique, Mixing by diffusion, Body fluids, Small-angle X-ray scattering
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ID: 5881250