Posted 07 August 2004 - 07:57 PM
I will hope to express virus protein with a high Molecular weight about 186kD. Somebody once tried to express via E.Coli system, but failed to do so. We hope to express this protein and make it crystallization. Would you be so kindly to give me some advice about this experiment, such as which expression system shall be used, and someone said the high MW protein is more easily to aggregate, thus how to avoid this disadvantagement.
Thanks in advance!
Posted 09 August 2004 - 11:48 AM
Posted 09 August 2004 - 04:35 PM
It is a RDRP in one plant virus. Do you think glycosylation or disulfide bond will affect the protrein's expression.
We have tried the cell free system for translation in vitro, and the result revealed it worked well.
Do you think some protein can not be expressed in E.Coli at all.
Posted 10 August 2004 - 03:11 AM
Posted 11 August 2004 - 04:48 PM