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." <[EMAIL PROTECTED]> >Subject: [SPAM:#] [ccp4bb] O/T: can a protein which dimerizes in solution crystallize as a monomer? >To: [email protected] > >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
