Hi Theresa,
A well known method to investigate the surroundings of metals in proteins
(metal-protein distances etc. ) is EXAFS (Extended X-ray Absorption Fine
Structure). It has been implemented in quite a few specialized synchrtoron beam
lines since the early 80s. I'm sure there's plenty of literature on the method
and results on many metal proteins (I'm familiar with the EXAFS results on
haemoglobin which caused quite a stir at the time).
Cheers,
Boaz
Boaz Shaanan, Ph.D.
Dept. of Life Sciences
Ben-Gurion University of the Negev
Beer-Sheva 84105
Israel
E-mail: bshaa...@bgu.ac.il
Phone: 972-8-647-2220 Skype: boaz.shaanan
Fax: 972-8-647-2992 or 972-8-646-1710
________________________________________
From: CCP4 bulletin board [CCP4BB@JISCMAIL.AC.UK] on behalf of Theresa Hsu
[theresah...@live.com]
Sent: Wednesday, May 09, 2012 9:02 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] Anomalous SAXS
Dear all
Is there any interesting aspects of metal proteins that can be used with
anomalous SAXS similar to MAD in MX? Can metal distance be measured with
time-resolved method (ligand binding and so on)? I knnow examples for materials
like nanoparticles but how about proteins?
Thank you.
