I saw also a great domain (around 150aa) movement on one of the subunits when crystals of the protein (yeast acetylglutamate kinase) were soaked with its inhibitor (arginine):
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0034734

2012/10/9 Alan Cheung <[log in to unmask]>
Depends on what you mean by large, but we saw very obvious domain movement when we soaked a protein (transcription factor TFIIS) into crystals of RNA Polymerase II (PMIDs 12914699/21346759/22726432).  We recently animated this conformational change, and you can watch it at:

http://www.youtube.com/watch?v=WlMV_l88Lus

...fast forward to about 5 mins 20 second to watch TFIIS binding.  And, er, sorry for the shameless plug ;)

Alan





On 09/10/2012 15:33, WENHE ZHONG wrote:
Dear CCP4 members,

Recently, I got a ligand soaking structure to clearly show a large
domain (~100 amino acids) movement compared to the no soaking structure.
Although there are some reported examples of this enzyme to suggest the
flexibility of this large domain which is relevant to substrate binding.
_But it is the first time I can see it happen in crystal soaking
procedure._ In this case, I am pleased by this result.


My question is, do you have any other example like mine, where domain
(or loop) movement is observed _*in crystal*_ during ligand _*soaking*_

procedure? It would be very helpful for me to relate my result to other
similar examples. Thank you very much.

King regards,
Wenhe

--
Alan Cheung
Gene Center
Ludwig-Maximilians-University
Feodor-Lynen-Str. 25
81377 Munich
Germany
Phone:  +49-89-2180-76845
Fax:  +49-89-2180-76999
E-mail: [log in to unmask]