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Hena, I think this notion of fold families having similar crystallization conditions has been kicking around since the 80's at least. I seem to recall Gary Gilliland presenting a fairly comprehensive and well controlled study for myoglobins and showing some correlation of crystallization conditions. However, I believe this example is an exception. Just to add to what Janet and Enrico have said: Taking the HIV integrase example from David Davies; or any of the Derewenda surface entropy reduction, protein engineering, examples; it is clear that small changes (even single point mutations) can dramatically alter the bulk properties (and crystallization behavior) of a protein. One last point, it is very hard to control for investigator preference when probing a database of successes. It may be that a review of the BMCD will reveal a correlation between crystallization conditions and fold families, but that could be due to a preference for particular crystallization conditions used in crystallization screens rather than properties of the protein family. Brent Brent W. Segelke Senior Biomedical Scientist Lawrence Livermore National Laboratory 7000 East Avenue, Livermore CA, 94550 USA [log in to unmask]<mailto:[log in to unmask]> From: CCP4 bulletin board [mailto:[log in to unmask]] On Behalf Of Janet Newman Sent: Wednesday, July 24, 2013 9:23 AM To: [log in to unmask] Subject: Re: [ccp4bb] database of crystallization condition Dear Hena, The BMCD might be a resource worth investigating: http://xpdb.nist.gov:8060/BMCD4/index.faces Although there are claims that structurally similar proteins may crystallise under similar conditions (the existence of directed screens -such as the Jena Biosciences 'Kinase' screen, you have to wonder (as Enrico points out) how these can work, as the bits that change the most in any protein family are the outside bits (ie, away from the active site) and thus are generally the parts going to affect crystallisation the most. Janet Janet Newman Principal Scientist / Director, Collaborative Crystallisation Centre CSIRO Material Science and Engineering 343 Royal Parade Parkville. VIC. 3052 Australia Tel +613 9662 7326 Email [log in to unmask]<mailto:[log in to unmask]> ________________________________ From: CCP4 bulletin board [[log in to unmask]] on behalf of Hena Dutta [[log in to unmask]] Sent: 25 July 2013 00:36 To: [log in to unmask]<mailto:[log in to unmask]> Subject: [ccp4bb] database of crystallization condition Hi, Can anyone tell, if there is any database containing the crystallization conditions of published structures? I want to see the conditions people have used for those proteins having some structural similarity. Any suggestion would be appreciated. Regards... Hena