The problem with crystallization is that is selects for the least
soluble, most packable species. Sometimes that works against what you
would like to know. That could include oligomerization state as well as
conformational state. For example, some of the allosteric carbonic
anhydrases stubbornly crystallize only in the T-state, despite
crystallization conditions that are known to preferentially stabilize
the R-state, and for which the predominant R-state population can be
confirmed by other methods.
Cheers,
_______________________________________
Roger S. Rowlett
Gordon & Dorothy Kline Professor
Department of Chemistry
Colgate University
13 Oak Drive
Hamilton, NY 13346
tel: (315)-228-7245
ofc: (315)-228-7395
fax: (315)-228-7935
email: [email protected]
On 4/8/2015 9:07 AM, Sebastiaan Werten wrote:
Dear all,
we are currently working on a protein that is known to exist in a
monomer-dimer equilibrium. At the high concentrations used for
crystallisation assays, the dimer is predominant and the monomer
practically undetectable.
Nevertheless, one of the crystal forms that we have obtained contains
the monomeric species, not the dimer.
I was wondering if anyone is aware of similar (published) cases, and
if the phenomenon as such has been discussed in detail anywhere?
I did literature searches but so far couldn't find anything.
Any pointers would be much appreciated!
Best wishes,
Sebastiaan Werten.
