Spring til hovednavigation Spring til søgning Spring til hovedindhold

Automated microfluidic sample-preparation platform for high-throughput structural investigation of proteins by small-angle X-ray scattering

  • Josiane P. Lafleur
  • , Detlef Snakenborg
  • , S.S. Nielsen
  • , J.P. Kutter
  • , L. Arleth
  • , M. Mller
  • , K.N. Toft
  • , B. Vestergaard
  • , A. Menzel
  • , J.K. Jacobsen

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Abstract

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.
OriginalsprogEngelsk
TidsskriftJournal of Applied Crystallography
Vol/bind44
Udgave nummer5
Sider (fra-til)1090-1099
Antal sider10
ISSN0021-8898
DOI
StatusUdgivet - 1 okt. 2011
Udgivet eksterntJa

Citationsformater