Thanks!
Phoebe
At 05:56 PM 1/22/2007, you wrote:
Hi Pheobe,
I remember an interesting paper that described how a structure revealed a
surprising role the buffer was playing in inhibition:
The 1.20 A resolution crystal structure of the aminopeptidase from
Aeromonas proteolytica complexed with tris: a tale of buffer inhibition.
* Desmarais WT,
* Bienvenue DL,
* Bzymek KP,
* Holz RC,
* Petsko GA,
* Ringe D.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=12176384
-----Original Message-----
From: CCP4 bulletin board on behalf of [EMAIL PROTECTED]
Sent: Mon 1/22/2007 3:29 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: : misbound ligand examples?
A biochemist friend asked for examples of cases were a protein was
co-crystallized with or soaked in a ligand that bound in the wrong place -
say, because the ligand used wasn't quite the right one or because other
important ligands were absent.
I'm sure such examples are out there, especially when soaks were done at
high concentrations, but I'm having trouble thinking of concrete examples.
Help?
thanks,
Phoebe Rice
---------------------------------------------------------------------------------------------------------------------------
Phoebe A. Rice
Assoc. Prof., Dept. of Biochemistry & Molecular Biology
The University of Chicago
phone 773 834 1723
fax 773 702 0439
http://bmb.bsd.uchicago.edu/index.html
http://www.nasa.gov/mission_pages/cassini/multimedia/pia06064.html
---------------------------------------------------------------------------------------------------------------------------
Phoebe A. Rice
Assoc. Prof., Dept. of Biochemistry & Molecular Biology
The University of Chicago
phone 773 834 1723
fax 773 702 0439
http://bmb.bsd.uchicago.edu/index.html
http://www.nasa.gov/mission_pages/cassini/multimedia/pia06064.html
