Hello, 
this looks like beta-mercaptoethanol adduct through a S-S bond. 
See 
[ https://pubmed-ncbi-nlm-nih-gov.insb.bib.cnrs.fr/12421561/ | The crystal 
structure of the Epstein-Barr virus protease shows rearrangement of the 
processed C terminus.  ] 
Buisson M, Hernandez JF, Lascoux D, Schoehn G, Forest E, Arlaud G, Seigneurin 
JM, Ruigrok RW, Burmeister WP. J Mol Biol. 2002 Nov 15;324(1):89-103. doi: 
10.1016/s0022-2836(02)01040-9. 

Wim 

De: "Liliana Margent" <[email protected]> 
À: "CCP4BB" <[email protected]> 
Envoyé: Lundi 18 Décembre 2023 18:03:46 
Objet: [ccp4bb] extra Fo-Fc density in two Cysteines 

Hi there, We’ve been having an issue in trying to clear regions of Fo-Fc 
density from a few cysteines during the refinement process. We were wondering 
if anyone had seen something similar so they could offer some insight on the 
likely chemistry at hand, and a potential refinement solution. Attached are two 
images of the observed extra density at two cysteines, 505 and 518. We have 
modeled acetylated cysteine, s-hydroxycysteine, and s-mercaptocysteine but it 
does not solve the density. The protein in question is a Protein Tyrosine 
Phosphatase known as STEP (PTPN5), with data collected to a resolution of 1.79 
Å. The crystals were grown in bis-tris pH 6.65, 200mM Li2SO4, ~30% PEG3350. Of 
note, prior to data collection the crystal was conserved at room temp for long 
time where it dried, and was subsequently rehydrated with mother liquor. Thank 
you so much. 



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Professor 
Institut de Biologie Structurale (IBS) CIBB 
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