Mass action is on the crystal's side.
Two recent examples of proteins that are dimers by standard
solution assays, but form weak/transient/co-factor-dependent
tetramers to function, and those tetramers are seen in the
crystal. (There is good solution data to back up the
relevance of the tetramer in both cases).
Yuan P, Gupta K, Van Duyne GD. Tetrameric structure of a
serine integrase catalytic domain. Structure. 2008 Aug
6;16(8):1275-86.
Mouw KW, Rowland SJ, Gajjar MM, Boocock MR, Stark WM, Rice PA.
Architecture of a serine recombinase-DNA regulatory complex.
Mol Cell. 2008 Apr 25;30(2):145-55.
Phoebe
==========================================
---- Original message ----
>Date: Thu, 11 Dec 2008 10:09:33 -0600
>From: "Santarsiero, Bernard D." <[log in to unmask]>
>Subject: [SPAM:#] [ccp4bb] O/T: can a protein which dimerizes
in solution crystallize as a monomer?
>To: [log in to unmask]
>
>In parallel with the discussion around this off-CCP4-topic,
are they any
>good examples of the opposite case, where the protein is a
monomer in
>solution (as evident from light scattering, MW determination
through
>centrifugation, EPR, etc.) but crystallizes as a dimer or
higher multimer?
>
>Bernie Santarsiero
Phoebe A. Rice
Assoc. Prof., Dept. of Biochemistry & Molecular Biology
The University of Chicago
phone 773 834 1723
http://bmb.bsd.uchicago.edu/Faculty_and_Research/01_Faculty/01_Faculty_Alphabetically.php?faculty_id=123
RNA is really nifty
DNA is over fifty
We have put them
both in one book
Please do take a
really good look
http://www.rsc.org/shop/books/2008/9780854042722.asp
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