Re: [ccp4bb]: Q: disulphide reduction in protein structures

[Michael Hahn <michael.hahn@charite.de>]

***  For details on how to be removed from this list visit the  ***
***    CCP4 home page http://www.dl.ac.uk/CCP/CCP4/main.html    ***

Dear Wai,

reduced disulphide bonds can be an artefact of data collection.
This happens due to radiation damage at high energy synchrotron
sources and was described recently in Weik et al., (2000) PNAS 97, 623-628.

Michael


Yu Wai Chen wrote:

> ***  For details on how to be removed from this list visit the  ***
> ***    CCP4 home page http://www.dl.ac.uk/CCP/CCP4/main.html    ***
>
> Dear all,
>
> Sorry this is not a CCP4 question.
>
> Can buried (i.e. small or no solvent accessible surface area) disulphide
> bonds be reduced to cysteines in general?  I have a structure in which 2
> cysteines are in the right position to form a S-S bond but the electron
> density shows otherwise.  My protein was purified in reducing
> conditions.  However, from other evidences (structure homology), these
> should form S-S.  Does anyone know of any published structure that can
> shed light on my puzzle?  Thanks a lot.
>
> Wai
> --
> ===================================================================
> Yu Wai CHEN, Ph.D. ..................   email:ywc@mrc-lmb.cam.ac.uk
>  Centre for Protein Engineering,             tel:+44-(0)1223-402148
>  MRC Centre, Hills Rd, Cambridge CB2 2QH, UK fax:+44-(0)1223-402140
>  WWW homepage: http://www.mrc-cpe.cam.ac.uk/~ywc

--
Dr. Michael Hahn
Institut fuer Biochemie
Charite, Humboldt Universitaet  phone: +49 (0)30 2802 6229
Monbijoustr. 2,                 fax:   +49 (0)30 2802 6252
10117 Berlin, Germany           email: michael.hahn@charite.de