Hello, is the crystal form the same in both cases?

Best wishes, Jon Cooper.
[email protected]

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-------- Original Message --------
On 22/04/2025 10:03, Flavio Di Pisa  wrote:

> Dear community,
>
> I’ve observed differences when crystallizing the same protein using two 
> different setups: microbatch under (Al’s) oil and vapor diffusion sitting 
> drop.
>
> The protein crystallizes in a condition containing 50 mM cadmium as one of 
> the precipitating agents. In the sitting drop setup, I observe 2 well-defined 
> cadmium ions at the so-called mineralization site (please see PDB entry 5lg8 
> and the related paper: https://www.pnas.org/doi/10.1073/pnas.1614302114), 
> with occupancies close to 1, as confirmed by the anomalous signal, plus other 
> "anomalous blob" near to this site.
>
> However, in the microbatch under oil setup, I never observe these cadmium 
> ions. Instead, I consistently detect only one cadmium ion with high 
> occupancy, and occasionally a second one with lower occupancy.
>
> In summary, crystallizing the same protein using these two setups results in 
> different metal-binding behavior.
>
> My question is: could it be that in microbatch under oil, ions might diffuse 
> away from the mineralization site? Could this account for the reduced number 
> of cadmium ions observed? Additionally, and more importantly, could the 
> crystallization setup influence the soaking efficiency of other metals, such 
> as iron (the natural substrate of this protein)?
>
> I’ve attached two screenshots:
>
> -
>
> One (orange blob) represents the protein crystallized via vapor diffusion, 
> showing two well-defined anomalous peaks.
>
> -
>
> The other shows the same site in a crystal grown via microbatch, where only 
> one anomalous signal (in white) is visible.
>
> I hope I’ve been clear. Thank you in advance, and I wish you all a great day!
>
> Best regards,
> Flavio
>
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