Hi,
The closest example I can think of is the extra density that was found in the
groove of the MHC class I structure (Bjorkman et al., long time ago) which
turned out to be a peptide that was co-purified. As we all know, it turned out
to be one of the major findings of this study as it pointed to the way MHC's
recognize peptides.
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 Leonard Thomas
[lmtho...@ou.edu]
Sent: Thursday, July 19, 2012 1:12 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] peptide fragment
Hello All,
I have been working on a structure for one of the research groups here
and have come across a peptide fragment of about 10 residues. The
protein forms a tetramer and the peptide is found between two of the
monomers. The protein itself does not require a peptide for function
or formation for that matter. Has anyone come across similar things?
and have a reference. We are trying to figure out where it may have
come from. My best guess so far is from somewhere in the purification
though I have no idea how long the protein sat around before
crystallization.
Cheers,
Leonard Thomas Ph.D.
Macromolecular Crystallography Laboratory Manager
University of Oklahoma
Department of Chemistry and Biochemistry
Stephenson Life Sciences Research Center
101 Stephenson Parkway
Norman, OK 73019-5251
lmtho...@ou.edu
http://barlywine.chem.ou.edu
Office: (405)325-1126
Lab: (405)325-7571
