Here’s two examples of heterooligomers that crystallized in a lattice with an 
extra monomer of one of the proteins. In both cases this was an unexpected 
result, but easily explained due to the low micro molar affinities for the 
complex.

4PKY
2CJS

Diana

**************************************************
Diana R. Tomchick
Professor
Departments of Biophysics and Biochemistry
UT Southwestern Medical Center
5323 Harry Hines Blvd.
Rm. ND10.214A
Dallas, TX 75390-8816
diana.tomch...@utsouthwestern.edu<mailto:diana.tomch...@utsouthwestern.edu>
(214) 645-6383 (phone)
(214) 645-6353 (fax)

On Jan 31, 2020, at 9:23 AM, Kluenemann, Thomas 
<thomas.kluenem...@helmholtz-hzi.de<mailto:thomas.kluenem...@helmholtz-hzi.de>> 
wrote:


EXTERNAL MAIL

Dear all,

We recently solved a the structure of a small c-type cytochrome. We observed, 
that of the eleven chains in the asymmetric unit ten form 3D domain swapped 
dimers by exchanging an α-helix. The eleventh  chain is present as a monomer. 
Based on the anomalous iron signal and the chain tracing we are sure that no 
chain was missed.
I tried to find other examples in the PDB, were one crystal is made of 
different homo- or heterooligomers.  I only found proteins with partial 
occupied peptide binding sites, which is not what I am looking for. Does anyone 
know of a case were the presence of different homo- or heterooligomers is 
required to form the crystal?

Best regards,
Thomas Klünemann



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