Dear Sebastiaan,
we indeed found something very similar with selecase (see
http://www.ncbi.nlm.nih.gov/pubmed/25159620).
This is a highly specific metallopeptidase, which is also a metamorphic
protein that transits between several
stable states, among which only the monomer is the active species. W
I just wanted to disagree with Roger's word choice, but not his argument (this
is a "flame"-free response). Forget about "packing" and "packable" as there is
no outside force doing the work. The molecules are just falling into a local
energy minimum where favorable intra- and intermolecular in
Just for clarity: symmetry mates have been taken into account, the
dimer really doesn't show up in those crystals.
Seb.
At Wednesday, 08-04-2015 on 15:16 Marjolein Thunnissen wrote:
Hi
I guess you mean that the protein is a monomer in the asymmetric unit.
It is quite common for multimer
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 stubbornl
Sure - crystallization selects what packs, which may constitute a very minor
fraction of what you set up drops with. 1DUH is an example...
-Luca
> On Apr 8, 2015, at 15:08, Sebastiaan Werten
> wrote:
>
> Dear all,
>
> we are currently working on a protein that is known to exist in a
> monome
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 co
