Analytical Ultracentrifuge
The analytical ultracentrifuge (AUC) monitors sedimentation process of particles in solution, including proteins, nucleic acids, carbohydrates and polymers. By using different experimental setups, namely sedimentation velocity (SV) and sedimentation equilibrium (SE), the instrument is capable of determining molecular weights (hence, oligomeric states), sample purity, conformations, self- or hetero- association properties. The instruments in BCF are Beckman Coulter ProteomeLab XL-I. It has absorbance optics (190nm-800nm) and Rayleigh interference. Rayleigh interference optical system provides possibility for large molecules which sediment too fast for absorbance system or samples with no absorbance or high absorbance backgrounds. Furthermore, it offers wider dynamic ranges for association studies. Users may specify detection systems, Rayleigh Interference and/or absorbance, along with experimental methods, SV or SE, upon filing sample submission requests through BCF reservation system.
Important Notification:
* (2013-07-01) XL-I is ready for sample submission (SV or SE with Rayleigh interference and/or UV/VIS absorbance optics).
* (2012-10-30) XL-A is restored and ready for SV sample submission (UV/VIS detector only).
* (2012-10-11) XL-A is out of service because of low light intensity, possibly from dirty lamp or slit.
* (2012-07-31) The rotor drive of XL-I was badly damaged possibly because of a sensor malfunction. BCF will resume all AUC service when the problem is resolved.
Related Softwares
For buffer density and viscosity estimation: Sedntrep; For AUC data analysis: Sedfit, Sedphat, UltraScan, DCDT+ and SVEDBERG; For hydrodynamic modeling: US-SOMO, HYDROXXX.
Suggested Reading:
Beckman Coulter Lab Resources for ProteomeLab XL-A/XL-I Andrea Balbo and Schuck P, 2005, in: Protein-Protein Interactions: a molecular cloning manual 2nd ed., Chapter 14, Cold Spring Harbor Laboratory Press, 253-277. Lebowitz J, Lewis MS and Schuck P, 2002, Modern analytical ultracentrifugation in protein science: A tutorial review, Protein Science, 11, 2067-2079.