Dear Eleanor, sorry for the late reply. I found a similar case (id: 2OEF, Cys 92). I mutated the Cys to Ser, but it did not change anything (xtal conditions and quality remained the same). In solution the protein is a monomer. However, adding 1 mM DTT resulted in a significant increase in crystal quality (larger 3D crystals with better resolution). I don't know why, though...
Cheers, Johannes 2017-02-01 20:45 GMT+01:00 Tom Peat <tom.p...@csiro.au>: > Hello Eleanor, > > > We found some intermolecular vicinal disulfides recently that we think are > 'real'. This class of proteins forms tetramers and in one version we find > these intermolecular disulfides across molecules. We did some tests and > found that oxidation or reduction has an effect on the stability of the > protein. We also saw this was consistent across multiple space groups. If > you would like to have a look, they were just released: 5HY0, 5HY2, 5HY4. > > As a comparison to another protein in this fold class that doesn't have > the disulfide is 5HWE. > > > cheers, tom > > > Tom Peat > Proteins Group > Biomedical Program, CSIRO > 343 Royal Parade > Parkville, VIC, 3052 > +613 9662 7304 <+61%203%209662%207304> > +614 57 539 419 > tom.p...@csiro.au > ------------------------------ > *From:* CCP4 bulletin board <CCP4BB@JISCMAIL.AC.UK> on behalf of Eleanor > Dodson <eleanor.dod...@york.ac.uk> > *Sent:* Thursday, February 2, 2017 2:17 AM > *To:* CCP4BB@JISCMAIL.AC.UK > *Subject:* [ccp4bb] intermolecular dissulphides > > Does anyone know of examples of these? > I have found one - 2WQW with these SSBOND records > 2WQW > SSBOND 1 CYS A 206 CYS A 227 1555 6556 > 2.07 > SSBOND 2 CYS B 206 CYS B 227 1555 5556 > 2.15 > > We seem to have one but it would have to form after crystalisation? > > Eleanor > > >
