Recently there were few articles where synthetic symmetrization was used to 
enhance the crystallizability. proteins used were MBP, lysozyme and GFP to name 
a few. you can search for it. one of them is -
https://www.sciencedirect.com/science/article/pii/S0969212615002890

[https://ars.els-cdn.com/content/image/1-s2.0-S0969212615002890-fx1.jpg]<https://www.sciencedirect.com/science/article/pii/S0969212615002890>
A Suite of Engineered GFP Molecules for Oligomeric 
Scaffolding<https://www.sciencedirect.com/science/article/pii/S0969212615002890>
Applications ranging from synthetic biology to protein crystallization could be 
advanced by facile systems for connecting multiple proteins together i…
www.sciencedirect.com


Dhiraj
________________________________
From: CCP4 bulletin board <CCP4BB@JISCMAIL.AC.UK> on behalf of Frank von Delft 
<frank.vonde...@cmd.ox.ac.uk>
Sent: Friday, November 12, 2021 8:52 AM
To: CCP4BB@JISCMAIL.AC.UK <CCP4BB@JISCMAIL.AC.UK>
Subject: [External] [ccp4bb] High-order oligomers vs robust crystals - 
references?

Hello all

Two decades ago, I remember (!) much talk about a reason that bacterial
proteins crystallize "more easily" is that they tend to come as
oligomers (dimers and up), and that this internal symmetry made them
happier to crystallize.

Did anybody ever publish hard evidence?  Or even, is there a primary
citation for the idea?

Thanks
Frank

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