Hi Ivan,
We've had good luck with the addition of chloramphenicol ~1 hour prior to
harvest, as described in:
Carrió, M. M., and Villaverde, A. (2001) Protein aggregation as bacterial
inclusion bodies is reversible. FEBS Lett. 489, 29­33.
We usually combine this with lower temperature growth (20 C).
Best regards,
Mark

Mark A. Wilson
Associate Professor
Department of Biochemistry/Redox Biology Center
University of Nebraska
N118 Beadle Center
1901 Vine Street
Lincoln, NE 68588
(402) 472-3626
[email protected] 





On 10/17/14 7:51 AM, "xaravich ivan" <[email protected]> wrote:

>Dear cc4bb enthusiasts,
>
>This is slightly off topic but many protein crystallographers might be
>familiar with this problem.
>
>
>I have been trying to over-express a bacterial (non-E.Coli) protein  in
>E.Coli and more than 80% goest to inclusion bodies.
>
>
>
>I tried the following
>
>
>Lowering the IPTG concentration to 0.1mM (range test from 0.075 mM - 0.5
>mM)
>
>
>Cold shock for 30 minutes in ice before induction
>
>
>Slow rotation speed at 18 degrees O/N after induction
>
>
>While these steps helped a bit I still get about 50-60% of my protein in
>inclusion bodies.
>
>
>I would like to know what other steps do you suggest to enhance the yield
>in the soluble fraction (without changing the host strain or manipulating
>the DNA)
>
>
>Thanks in advance
>
>Ivan
>
>

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