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

TY - JOUR

T1 - Automated microfluidic sample-preparation platform for high-throughput structural investigation of proteins by small-angle X-ray scattering

AU - Lafleur, Josiane

AU - Snakenborg, Detlef

AU - Nielsen, Søren Skou

AU - Møller, Magda

AU - Toft, Katrine Nørgaard

AU - Menzel, Andreas

AU - Jacobsen, Jes K.

AU - Vestergaard, Bente

AU - Arleth, Lise

AU - Kutter, Jörg Peter

PY - 2011/10

Y1 - 2011/10

N2 - 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.

AB - 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.

U2 - 10.1107/S0021889811030068

DO - 10.1107/S0021889811030068

M3 - Journal article

SN - 0021-8898

VL - 44

SP - 1090

EP - 1099

JO - Journal of Applied Crystallography

JF - Journal of Applied Crystallography

ER -