If you can model it as a lysine, it will be the beta-ME adduct. There's a good
one in 1b4e (see attached) which Eileen Jaffe pointed out to me and I never got
round to sorting out. Now there's another one of 'mine' for which the data have
not been deposited, but I did put the images on zenodo 4 years ago
(https://doi.org/10.5281/zenodo.51560) if anyone fancies a little lock-down
project!!
On Friday, 27 March 2020, 22:02:20 GMT, CRAIG A BINGMAN
<[email protected]> wrote:
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]>
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 1/05Department of BiochemistryUniversity of LeicesterLancaster
RoadLeicester, LE1 9HN, U.K. Phone +44 (0) 116 229 7077
From: CCP4 bulletin board <[email protected]> on behalf of Paul Emsley
<[email protected]>
Sent: 27 March 2020 21:33
To: [email protected] <[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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