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Dan, how does your very hydrophobic protein function in the cell? Is it stabilized using a binding partner? if so, i recommend trying to crystallize the complex, if it is better behaved. Another approach might be to use a tag to increase the solubility. I think there are vectors available for this approach. yet, this could still lead to aggregation and similar problem. You say it is soluble with detergents. then you might simply have a facility do a high throughput screening of your protein at various concentrations. ---ATTN: Die-hard crystallographers please stop reading here.--- Do you have access to NMR facility? If so, another approach might be to do solution structure. but if you aren't familar with NMR, this may pose an even bigger problem, than any sort of solution, but should be kept in mind, should crystallography not work. Sorry I couldn't help more. Best of Luck! Cheers, Nick -----Original Message----- From: ferrarod <[EMAIL PROTECTED]> To: <[email protected]> Date: Tue, 31 Oct 2006 14:40:11 -0500 Subject: [ccp4bb]: Protein Crystallization Question *** For details on how to be removed from this list visit the *** *** CCP4 home page http://www.ccp4.ac.uk *** Hello everyone, Sorry for the off topic question. I was wondering if anyone had any ideas or suggestions on protein crystallization of a small peptide. It is 46 amino acids and it is very hydrophobic. It is not soluble in buffered water, but it is soluble in 70% acetonitrile and in detergent. We have tried traditional sparse matrix screens, but we get precipitate even at low concentrations (i.e. 3 mg/ml). Any advice or suggestions would be appreciated. Cheers, Dan ________________________________________ Nicholas Noinaj University of Kentucky College of Medicine Department of Molecular and Cellular Biochemistry The Center for Structural Biology Biomedical Biological Sciences Research Building, Rm 236 741 S. Limestone Lexington, Ky 40536 Lab: 859-323-8183 Cell: 859-893-4789 Home: 859-228-0978 [EMAIL PROTECTED] noinaj.com
