Hi Prem,
besides trying surface entropy reduction you can also start by analyzing your
crystal contacts and mutate residues therein. This was for example
investigated in the 90's by GE Schulz and coworkers.
Good Luck
Alex
Dr. Alexander Pautsch
Boehringer Ingelheim Pharma GmbH &
Have you solved the structure? It's just that you don't say why you need
different crystal forms.
We had to do a bit of "crystal engineering" in order to get a complex between
our protein and a peptide. It turned out to be relatively simple case; visually
inspecting the crystal packing (in Coot
http://services.mbi.ucla.edu/SER/
but no space group predictions are possible. BR
From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of Prem
Kaushal
Sent: Tuesday, February 14, 2012 3:36 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] surface residue mutation
Hi
W
Hi
We have a protein that crystallized in P21212 space group. We are looking
for some different crystal forms. We tried few things did not work. Now we
are thinking to mutate surface residues. Anybody aware of any software
which can predict the mutations that might help in crystallizing protein in
Folks
The latest issue of the Computational Crystallography Newsletter is
available on-line at http://www.phenix-online.org/newsletter for
download. The articles are of general interest to protein
crystallographers and are listed below.
Enjoy
Nigel Moriarty
Articles
CCTBX tools for derivativ
Hi,
I'm just writing to ask whether anybody has experienced the same problem
as me concerning mutation of Methionines (MET) to Seleno-Methionines
(MSE).
When I change the MET residues to MSE residues and do real space refine,
the chain goes completely bizerk and the MSE residue (and most of the
r
