Could it not just be classical radiation damage, that is known to love
breaking SS bonds? If I understood correctly, single-particle cryo-EM
inflicts much higher radiation doses than X-ray crystallography.

Best wishes,

Gerard.

--
On Wed, Dec 22, 2021 at 09:51:59AM +0000, Weiergräber, Oliver H. wrote:
> Hmm, this may indeed be a disulfide bond, but the sulfur atoms do not seem to 
> occupy their density centroids.
> They could be either _pushed_ apart by the refinement algorithm (which one 
> are you using?) or _pulled_ apart due to incorrect geometry in their 
> neighbourhood.
> 
> Cheers
> Oliver
> 
> ==================================================
>   PD Dr. Oliver H. Weiergräber
>   Institut für Biologische Informationsprozesse
>   IBI-7: Strukturbiochemie
>   Tel.: +49 2461 61-2028
>   Fax: +49 2461 61-9540
> ==================================================
> 
> 
> ________________________________________
> From: CCP4 bulletin board [[email protected]] on behalf of Hochberg, 
> Georg [[email protected]]
> Sent: 22 December 2021 10:06
> To: [email protected]
> Subject: [ccp4bb] Strange cysteines
> 
> Dear CCP4ers,
> 
> 
> We have recently solved the structure of an enzyme by cryoEM, which has two 
> cysteines at its dimer interface, one in each monomer. The density around 
> these two cysteines is very odd (see picture). They are too far apart for a 
> disulphide bond, and there is nothing around these two cysteines that could 
> help coordinate a metal. This density is also not a result of symmetry 
> constraints in the density refinement either.  We'd be very grateful for any 
> ideas.
> 
> [cid:b92417da-97f2-4dc3-9b5c-92278a5318fd]
> 
> 
> All the best and happy holidays,
> 
> Georg Hochberg
> 
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