TY - JOUR

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

A1 - Lafleur,Josiane P.

A1 - Snakenborg,Detlef

A1 - Nielsen,Søren Skou

A1 - Møller,Magda

A1 - Toft,Katrine N.

A1 - Menzel,Andreas

A1 - Jacobsen,Jes K.

A1 - Vestergaard,Bente

A1 - Arleth,Lise

A1 - Kutter,Jörg Peter

AU - Lafleur,Josiane P.

AU - Snakenborg,Detlef

AU - Nielsen,Søren Skou

AU - Møller,Magda

AU - Toft,Katrine N.

AU - Menzel,Andreas

AU - Jacobsen,Jes K.

AU - Vestergaard,Bente

AU - Arleth,Lise

AU - Kutter,Jörg Peter

PY - 2011

Y1 - 2011

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. © 2011 International Union of Crystallography.

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. © 2011 International Union of Crystallography.

KW - High-throughput

KW - UV absorbance

KW - Mixing efficiency

KW - Automated data analysis

KW - Structural analysis

KW - Automation

KW - Model proteins

KW - Hardware and software

KW - Data reduction

KW - Structural investigation

KW - Fluidic control

KW - Protein structure

KW - Microfluidics

KW - Scattering

KW - X ray scattering

KW - Bovine serum albumins

KW - Sample consumption

KW - Proteins

KW - High-throughput technique

KW - Mixing by diffusion

KW - Body fluids

KW - Small-angle X-ray scattering

U2 - 10.1107/S0021889811030068

DO - 10.1107/S0021889811030068

JO - Journal of Applied Crystallography

JF - Journal of Applied Crystallography

SN - 00218898

IS - 5

VL - 44

SP - 1090

EP - 1099

ER -