My guess would be that the chains were prepared under reducing conditions, 
mixed, and then allowed to oxidize. The surface adduct could easily form during 
this process.

On Mar 27, 2020, at 4:38 PM, Cowan, Richard H. (Dr.) 
<[email protected]<mailto:[email protected]>> wrote:

Hi,

The Fab constructs have a c-terminal cysteines on both the heavy and light 
chains, which should form a disulphide. Adding reducing agent to the 
purification of the protein would potentially reduce this disulphide, possible 
causing issues the stability and heterogeneity? At least that's my 
understanding?

Thanks,

Dr Richard Cowan
Research Associate

HWLSB 1/05
Department of Biochemistry
University of Leicester
Lancaster Road
Leicester, LE1 9HN, U.K.

Phone +44 (0) 116 229 7077

________________________________
From: CCP4 bulletin board <[email protected]<mailto:[email protected]>> 
on behalf of Paul Emsley 
<[email protected]<mailto:[email protected]>>
Sent: 27 March 2020 21:33
To: [email protected]<mailto:[email protected]> 
<[email protected]<mailto:[email protected]>>
Subject: Re: [ccp4bb] Covalent Cysteine Aduct


On 27/03/2020 21:06, Cowan, Richard H. (Dr.) wrote:


  although [BME] seems unlikely, since the crystallized protein is a Fab.


I don't follow.


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