Hi Jon,
Thanks for the reply. I don't think this is acetylation, because I only see
this density in the crystals that grew with malonate. In other conditions
doesn't show anything like that. So I thought it'd be the malonate. But
I'll check on that.
Thanks for the suggestion.

Kind regards
Ana

On Mon, 16 Aug 2021 at 16:56, Jon Cooper <jon.b.coo...@protonmail.com>
wrote:

> Hello, could the His be partially acetylated?
>
> Best wishes Jon.C.
>
>
> Sent from ProtonMail mobile
>
>
>
> -------- Original Message --------
> On 16 Aug 2021, 14:52, Ana Ebrecht < anaebre...@gmail.com> wrote:
>
>
> Dear all,
>
> I am building the structure of a protein that was crystallized in 0.2 M
> sodium malonate pH 5.0, 20% w/v polyethylene glycol 3,350.
> During the refinement, we found what we think is a malonate molecule in
> the active site, but it seems like is bound somehow to the histidine
> (this His is the catalytic residue of the enzyme), almost like a covalent
> interaction. Under other conditions of crystallization, the protein bound
> a sulfate and an acetate in the site but did not show this type of
> interaction with the histidine.
>
> We couldn't find anything that explains a reaction between the malonate
> and the histidine.
> Does anyone have experience with this reaction or have seen something
> similar before?
>
> Thanks
> Kind regards
> Ana
>
>
>
>
>
> [image: malonate.jpg]
>
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