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I am starting to work on a large protein complex ( about 1 mega dalton) that requires some detergent during the last purification steps and during protein concentration to keep it in solution. Even then, we were only able to concentrate it to about 1 mg/ml. I just took over the project and wanted to characterize the protein for solubility and DLS under various buffer conditions. Looking at protein drops under the microscope, I noticed that there is phase separation in the protein solution even at 0.5 mg/ml protein. The protein is in 20 mM buffer, 0.25 M KCl, 5% glycerol, 0.25% beta-octylglucoside. I will probably not be able to measure DLS on such a sample and I expect it to be a problem for crystallization as well. Any suggestions what to try to get a more homogeneous protein solution.
Thanks Ursula
