| Quick navigation: | Home | Site Map || References | Biography || Copyright | Other copyright | Contact us | Advert | | |
Re: [ccp4bb] Reg. Protein purification |
||
- Protein crystallographyMain steps:- Protein purification- Crystallisation Special:- Programs for crystallography- X-ray detectors Basic tutorials:- Chemistry- Protein - Peptide - Amino Acids Xtal community:- CCP4BB |
CCP4bb navigationCCP4bb <-- 1999 <-- November 1999 <-- 30 November 1999Subject: Re: Reg. Protein purification From: Jacob Keller j-keller2 {- at -} MD {- dot -} NORTHWESTERN {- dot -} EDU Date: 2010-01-08 Why don't you do a blast search in the human proteome to see whether there is a human ortholog to the bacterial protein you co-purified, and consider also whether the interaction would make any sense physiologically, of course. It might be that you have discovered something interesting! Jacob ******************************************* Jacob Pearson Keller Northwestern University Medical Scientist Training Program Dallos Laboratory F. Searle 1-240 2240 Campus Drive Evanston IL 60208 lab: 847.491.2438 cel: 773.608.9185 email: j-keller2@northwestern.edu ******************************************* On Jan 8, 2010, at 7:41 AM, Sivaraman Padavattan wrote: Dear all, I am trying to express the human protein using bacterial expression strain (Rosetta) and purified using Ni-NTA affinity purification. The Molecular weight of out protein is 47 kDa. In SDS-PAGE, we have seen that 27 kDa contaminant protein co-eluted with our protein even at high concentration of Imidazole. In Superose 12 column, these two proteins eluted as a single peak and its corresponding molecular weight suggestive of partial interaction. By mass mapping we have found 27 kDa band is an adenylate kinase. Is there any specific way to separate adenylate kinase from our protein? Thanks in advance, Sivaraman Padavattan CCP4bb navigationCCP4bb <-- 1999 <-- November 1999 <-- 30 November 1999 |
|
| ProteinCrystallography.org: Copyright 2006-2010 by Quid United Ltd |