Hi,
Your idea does sound really crazy but actually Jacob had made a very good
valid point.
Question is do you think your aggregate still functioning or not, if not,
can you revive them in vitro and how effective is your refolding process if
you are going to refold them?
You may want to take a loo
Hello,
The information you provided to us here is not enough. there are so many
parameters and
so many means to optimize 2D crystal. All of which depends on what kind of
protein you
are working on (membrane associated or soluble) and what kind of technique that
you use
to grow your crystal (l
exists in solution as a dimer.
> The technique is hanging drop, vapor diffusion. And the mother liquor is
> ~ 0.1 mM cacodylate pH 6.2ish, MgCl2 and PEG 20k.
>
> =v=
>
>
> -Original Message-
> From: Puey Ounjai
> To: CCP4BB@JISCMAIL.AC.UK
> Sent: Fri, 9 Jan
Hi Kien,
As Artem pointed out earlier. Are you sure that your protein folded
correctly. You want to make sure that the protein is expressed in lipid
membrane not in inclusion body. If so, considering changing the host might
be a good idea.
Also, did you use any kind of detergent when you extract
In fact, I agree with Artem that detergent can be very difficult to get rid
of. It totally depend on the property of detergent. In your case that the
protein has no transmembrane region. You probably dont need much detergent
in your solution to keep your protein happy. I dont think having detergent
