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: [log in to unmask]
Phone: 972-8-647-2220 Skype: boaz.shaanan
Fax: 972-8-647-2992 or 972-8-646-1710
________________________________________
From: CCP4 bulletin board [[log in to unmask]] on behalf of Theresa Hsu [[log in to unmask]]
Sent: Wednesday, May 09, 2012 9:02 PM
To: [log in to unmask]
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.
