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Hello, why would you want to make your protein less soluble? Do you not have enough material to carry out crystallisation trials at 120mg/ml? Anyhow, the best answer might be given by the screens you have undertaken. ANy condition where the protein precipitates is a condition that makes it less soluble - that is the principle of hanging drop vapour diffusion. What are the current buffer conditions? You can alter the pH (although at extremes this might introduce drastic conformational changes), try salting-out, change the temperatur, etc. Does your protein stay in solution at all these conditions? -- Tim Gruene Institut fuer anorganische Chemie Tammannstr. 4 D-37077 Goettingen GPG Key ID = A46BEE1A On Fri, 3 Feb 2006, OnLineHelpForm wrote: > I am using ccp4 version release-6_0. > I am using ccp4i. > My compiler is: native > I installed using compilesource > The problem is as follows: > Hello. I have a very stable protein (non-membrane) according to DLS results, > and according to pre-crystallization screening from Hampton, I have a very > soluable protein (concentrated up to 124 mg/mL). This is consistent with the > crystallization probelms I have been having (ie no crystals). I have read > articles about mutating and methylating the protein, but this sounds risky > and possibly undesirable. Any information about making this protein less > soluable without distrubing the folding for crystallization would be very > much appreciated. Thank you! CSides ([EMAIL PROTECTED]) > > I have done the following patches: > No - but I will go back and check them now! > > > Thanks in advance, > CSides, [EMAIL PROTECTED] >
