A and B unit cell dimensions are hardly bigger than twice the uni cell of cubic 
NaCl and will probably not accommodate a 30 kDa protein.

Make a SDS gel of washed & dissolved crystals to be sure these are not alt or 
inhibitor crystals. You can stain the crystals with IzIt...

J.

--
Dr. math. et dis. nat. Jeroen R. Mesters
https://orcid.org/0000-0001-8532-6699



University of Lübeck
Institute of Biochemistry
https://www.biochem.uni-luebeck.de
phone: +49-451-3101-3105
Ratzeburger Allee 160
23562 Lübeck
Germany
--

> Am 03.02.2023 um 09:22 schrieb kavyashreem <[email protected]>:
> 
> Dear all,
> 
> We crystallized a protein (30kDa) + ligand (by cocrystallization), in the 
> condition 10%PEG3350, 50mM Zinc acetate.
> Protein was in the buffer 20mM HEPES, 150mM NaCl, 1uM ZnCl2, 4mM TCEP, pH 8. 
> Crystal:                             Crystal:                           
> crystal under UV m
> <b06fc576.png>     <e091c7fd.png>   <8ef9453e.png>
> When we collected the data at an in-house facility, it looked something like 
> this:
> <b903961d.png>
> The minimum resolution spot is around 9Ang and maximum ~2.2Ang. 
> I have not come across a protein diffraction like this, nor of a salt. When I 
> ran the gel for the incubated protein (protein+ligand), there was no 
> degradation.
> Although, I was sure there is some problem with this image I tried 
> processing, which could not be, But indexing showed a unit cell  of 11Ang, 
> 11Ang, 46Ang in P3. which was quite expected for two of the axes but not the 
> third.
> Can anyone please shed some light on this diffraction image?
> How can it happen?
>  
> Thank you
> Regards
> Kavya
>  
> 
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